ARO1 encodes the pentafunctional AROM polypeptide of Saccharomyces cerevisiae, a 1588-residue cytosolic homodimeric enzyme that is a fusion of five domains homologous to the monofunctional E. coli shikimate-pathway enzymes AroB, AroA, AroK/L, AroD and AroE. AROM catalyses steps 2-6 of the seven-step shikimate pathway that converts DAHP into EPSP: 3-dehydroquinate synthase (EC 4.2.3.4), 3-dehydroquinate dehydratase (type I, EC 4.2.1.10), shikimate dehydrogenase (NADP+, EC 1.1.1.25), shikimate kinase (EC 2.7.1.71) and EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase, EC 2.5.1.19). Chorismate, produced from EPSP by ARO2, is the common precursor of phenylalanine, tyrosine, tryptophan, p-aminobenzoate and p-hydroxybenzoate. The DHQ synthase domain binds Zn2+, and ARO1 expression is co-ordinately controlled by the GCN4 general amino acid control system. aro1 mutants are aromatic amino acid auxotrophs and homozygous aro1 diploids fail to sporulate.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: IEA from InterPro2GO mapping (InterPro:IPR013792). Generic 'catalytic activity' adds nothing beyond the five specific AROM activities already annotated with experimental support. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic |
| GO:0003855 3-dehydroquinate dehydratase activity | IDA PMID:6355828 Isolation of the ARO1 cluster gene of Saccharomyces cerevisi... | ACCEPT | Summary: IDA annotation from PMID:6355828. Larimer et al. cloned ARO1 and showed that ARO1 transformants overproduce all five AROM activities, including 3-dehydroquinate dehydratase, and complement the corresponding E. coli aro mutants. This is one of the five core catalytic activities of AROM (type I dehydroquinase (step 3, fourth domain)). Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003855 3-dehydroquinate dehydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (ARBA:ARBA00027694; InterPro:IPR001381, InterPro:IPR008289, InterPro:IPR018508; RHEA:21096; EC:4.2.1.10; UniRule:UR000166141). The 3-dehydroquinate dehydratase activity is carried by the type I dehydroquinase (step 3, fourth domain) of AROM; the family assignment is correct for this protein and is backed by the IDA from PMID:6355828. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003855 3-dehydroquinate dehydratase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. YeastPathways assigns the 3-dehydroquinate dehydratase reaction to ARO1 in this pathway; correct, as the type I dehydroquinase (step 3, fourth domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003855 3-dehydroquinate dehydratase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. YeastPathways assigns the 3-dehydroquinate dehydratase reaction to ARO1 in this pathway; correct, as the type I dehydroquinase (step 3, fourth domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003855 3-dehydroquinate dehydratase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. YeastPathways assigns the 3-dehydroquinate dehydratase reaction to ARO1 in this pathway; correct, as the type I dehydroquinase (step 3, fourth domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003856 3-dehydroquinate synthase activity | IDA PMID:6355828 Isolation of the ARO1 cluster gene of Saccharomyces cerevisi... | ACCEPT | Summary: IDA annotation from PMID:6355828. Larimer et al. cloned ARO1 and showed that ARO1 transformants overproduce all five AROM activities, including 3-dehydroquinate synthase, and complement the corresponding E. coli aro mutants. This is one of the five core catalytic activities of AROM (DHQ synthase (step 2, N-terminal domain)). Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003856 3-dehydroquinate synthase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (InterPro:IPR008289, InterPro:IPR016037; RHEA:21968; EC:4.2.3.4; UniRule:UR000166141). The 3-dehydroquinate synthase activity is carried by the DHQ synthase (step 2, N-terminal domain) of AROM; the family assignment is correct for this protein and is backed by the IDA from PMID:6355828. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003856 3-dehydroquinate synthase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. YeastPathways assigns the 3-dehydroquinate synthase reaction to ARO1 in this pathway; correct, as the DHQ synthase (step 2, N-terminal domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003856 3-dehydroquinate synthase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. YeastPathways assigns the 3-dehydroquinate synthase reaction to ARO1 in this pathway; correct, as the DHQ synthase (step 2, N-terminal domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003856 3-dehydroquinate synthase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. YeastPathways assigns the 3-dehydroquinate synthase reaction to ARO1 in this pathway; correct, as the DHQ synthase (step 2, N-terminal domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA placed at PANTHER:PTN000472635 with 4 with/from members (this gene's own experimental annotation is among them). The EPSP synthase activity is carried by the EPSP synthase (step 6, second domain) of AROM; the family assignment is correct for this protein and is backed by the IDA from PMID:6355828. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity | IDA PMID:6355828 Isolation of the ARO1 cluster gene of Saccharomyces cerevisi... | ACCEPT | Summary: IDA annotation from PMID:6355828. Larimer et al. cloned ARO1 and showed that ARO1 transformants overproduce all five AROM activities, including EPSP synthase, and complement the corresponding E. coli aro mutants. This is one of the five core catalytic activities of AROM (EPSP synthase (step 6, second domain)). Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (InterPro:IPR006264, InterPro:IPR008289; RHEA:21256; EC:2.5.1.19; UniRule:UR000166141). The EPSP synthase activity is carried by the EPSP synthase (step 6, second domain) of AROM; the family assignment is correct for this protein and is backed by the IDA from PMID:6355828. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. YeastPathways assigns the EPSP synthase reaction to ARO1 in this pathway; correct, as the EPSP synthase (step 6, second domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. YeastPathways assigns the EPSP synthase reaction to ARO1 in this pathway; correct, as the EPSP synthase (step 6, second domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. YeastPathways assigns the EPSP synthase reaction to ARO1 in this pathway; correct, as the EPSP synthase (step 6, second domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004764 shikimate 3-dehydrogenase (NADP+) activity | IDA PMID:6355828 Isolation of the ARO1 cluster gene of Saccharomyces cerevisi... | ACCEPT | Summary: IDA annotation from PMID:6355828. Larimer et al. cloned ARO1 and showed that ARO1 transformants overproduce all five AROM activities, including shikimate dehydrogenase, and complement the corresponding E. coli aro mutants. This is one of the five core catalytic activities of AROM (shikimate dehydrogenase (step 4, C-terminal domain)). Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004764 shikimate 3-dehydrogenase (NADP+) activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (InterPro:IPR008289, InterPro:IPR010110, InterPro:IPR013708; RHEA:17737; EC:1.1.1.25; UniRule:UR000166141). The shikimate dehydrogenase activity is carried by the shikimate dehydrogenase (step 4, C-terminal domain) of AROM; the family assignment is correct for this protein and is backed by the IDA from PMID:6355828. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004764 shikimate 3-dehydrogenase (NADP+) activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. YeastPathways assigns the shikimate dehydrogenase reaction to ARO1 in this pathway; correct, as the shikimate dehydrogenase (step 4, C-terminal domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004764 shikimate 3-dehydrogenase (NADP+) activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. YeastPathways assigns the shikimate dehydrogenase reaction to ARO1 in this pathway; correct, as the shikimate dehydrogenase (step 4, C-terminal domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004764 shikimate 3-dehydrogenase (NADP+) activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. YeastPathways assigns the shikimate dehydrogenase reaction to ARO1 in this pathway; correct, as the shikimate dehydrogenase (step 4, C-terminal domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004765 shikimate kinase activity | IDA PMID:6355828 Isolation of the ARO1 cluster gene of Saccharomyces cerevisi... | ACCEPT | Summary: IDA annotation from PMID:6355828. Larimer et al. cloned ARO1 and showed that ARO1 transformants overproduce all five AROM activities, including shikimate kinase, and complement the corresponding E. coli aro mutants. This is one of the five core catalytic activities of AROM (shikimate kinase (step 5, third domain)). Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004765 shikimate kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (ARBA:ARBA00027724; InterPro:IPR008289; RHEA:13121; EC:2.7.1.71; UniRule:UR000166141). The shikimate kinase activity is carried by the shikimate kinase (step 5, third domain) of AROM; the family assignment is correct for this protein and is backed by the IDA from PMID:6355828. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004765 shikimate kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. YeastPathways assigns the shikimate kinase reaction to ARO1 in this pathway; correct, as the shikimate kinase (step 5, third domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004765 shikimate kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. YeastPathways assigns the shikimate kinase reaction to ARO1 in this pathway; correct, as the shikimate kinase (step 5, third domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0004765 shikimate kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. YeastPathways assigns the shikimate kinase reaction to ARO1 in this pathway; correct, as the shikimate kinase (step 5, third domain) is part of AROM. Supporting Evidence: PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli PMID:2825635 the arom polypeptide is a mosaic of functional domains |
| GO:0005515 protein binding | IPI PMID:11805826 Functional organization of the yeast proteome by systematic ... | REMOVE | Summary: IPI annotation from PMID:11805826. High-throughput physical interaction from the Gavin et al. 2002 TAP-MS complex survey. 'Protein binding' conveys no function and the paper supports no more informative MF for AROM; the contact most likely reflects chaperone/client or co-purification association. Removal does not imply the interaction is false. Supporting Evidence: PMID:11805826 We used tandem-affinity purification (TAP) and mass spectrometry in a large-scale approach to characterize multiprotein complexes in Saccharomyces cerevisiae. file:yeast/ARO1/ARO1-uniprot.txt P08566; P15108: HSC82; NbExp=3; IntAct=EBI-2883, EBI-8666; |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: IPI annotation from PMID:15766533. High-throughput physical interaction from the Zhao et al. 2005 Hsp90 interaction map (UniProt lists HSC82 as an AROM interactor). 'Protein binding' conveys no function and the paper supports no more informative MF for AROM; the contact most likely reflects chaperone/client or co-purification association. Removal does not imply the interaction is false. Supporting Evidence: PMID:15766533 Physical, genetic, and chemical-genetic interactions centered on the conserved chaperone Hsp90 were mapped at high resolution in yeast file:yeast/ARO1/ARO1-uniprot.txt P08566; P15108: HSC82; NbExp=3; IntAct=EBI-2883, EBI-8666; |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: IPI annotation from PMID:16429126. High-throughput physical interaction from the Gavin et al. 2006 genome-wide complex screen. 'Protein binding' conveys no function and the paper supports no more informative MF for AROM; the contact most likely reflects chaperone/client or co-purification association. Removal does not imply the interaction is false. Supporting Evidence: PMID:16429126 Here we report the first genome-wide screen for complexes in an organism, budding yeast, using affinity purification and mass spectrometry. file:yeast/ARO1/ARO1-uniprot.txt P08566; P15108: HSC82; NbExp=3; IntAct=EBI-2883, EBI-8666; |
| GO:0005524 ATP binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: IEA from UniRule-based electronic annotation (UniRule:UR000166141). ATP is the phosphoryl donor for the shikimate kinase domain of AROM, so ATP binding is correct but is a substrate-binding feature subsumed by shikimate kinase activity. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt Reaction=shikimate + ATP = 3-phosphoshikimate + ADP + H(+); |
| GO:0005737 cytoplasm | HDA PMID:14562095 Global analysis of protein localization in budding yeast. | ACCEPT | Summary: HDA annotation from PMID:14562095. Genome-wide GFP localisation (Huh et al.) placed Aro1 in the cytoplasm. Supporting Evidence: PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories file:yeast/ARO1/ARO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA placed at PANTHER:PTN000472635 with 1 with/from members. Cytoplasmic localisation is ancestral for the AROM/shikimate enzymes. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (InterPro:IPR010110, InterPro:IPR016037; UniProtKB-SubCell:SL-0086; UniRule:UR000166141). AROM is a soluble cytosolic enzyme with no targeting signals; consistent with GFP data. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. AROM is a soluble cytosolic enzyme with no targeting signals; consistent with GFP data. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. AROM is a soluble cytosolic enzyme with no targeting signals; consistent with GFP data. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. AROM is a soluble cytosolic enzyme with no targeting signals; consistent with GFP data. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. |
| GO:0008270 zinc ion binding | RCA PMID:30358795 The cellular economy of the Saccharomyces cerevisiae zinc pr... | KEEP AS NON CORE | Summary: RCA annotation from PMID:30358795. Wang et al. compiled the yeast zinc proteome by bioinformatic prediction; AROM is included because its DHQ synthase domain is a Zn2+-dependent enzyme (two Zn2+ per subunit per HAMAP). Plausible cofactor binding, not a core function. Supporting Evidence: PMID:30358795 The yeast zinc proteome of 582 known or potential zinc-binding proteins was identified using a bioinformatics analysis file:yeast/ARO1/ARO1-uniprot.txt Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- |
| GO:0009073 aromatic amino acid biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (InterPro:IPR006264, InterPro:IPR008289, InterPro:IPR016037; UniRule:UR000166141). In GO, chorismate biosynthesis is not placed under aromatic amino acid biosynthesis, so this term separately captures that the shikimate trunk catalysed by AROM is required for synthesis of Phe, Tyr and Trp; aro1 mutants are aromatic auxotrophs. Supporting Evidence: PMID:1943992 Most reactions of this branched pathway are common to all organisms which are able to synthesize tryptophan, phenylalanine, and tyrosine. PMID:361708 Mutations in ARO1 and ARO2 genes coding for enzymes involved in the common part of the aromatic amino acid pathway |
| GO:0009073 aromatic amino acid biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways COMPLETE-ARO-PWY-1 ('superpathway of aromatic amino acid biosynthesis') GO-CAM conversion. In GO, chorismate biosynthesis is not placed under aromatic amino acid biosynthesis, so this term separately captures that the shikimate trunk catalysed by AROM is required for synthesis of Phe, Tyr and Trp; aro1 mutants are aromatic auxotrophs. Supporting Evidence: PMID:1943992 Most reactions of this branched pathway are common to all organisms which are able to synthesize tryptophan, phenylalanine, and tyrosine. PMID:361708 Mutations in ARO1 and ARO2 genes coding for enzymes involved in the common part of the aromatic amino acid pathway |
| GO:0009423 chorismate biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA placed at PANTHER:PTN000472635 with 3 with/from members. Chorismate biosynthesis is the pathway in which all five AROM activities act (steps 2-6 of 7). Supporting Evidence: PMID:1943992 Most reactions of this branched pathway are common to all organisms which are able to synthesize tryptophan, phenylalanine, and tyrosine. file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli |
| GO:0009423 chorismate biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from combined automated IEA pipeline (UniRule:UR000166141; UniPathway:UPA00053). AROM catalyses steps 2-6 of chorismate biosynthesis; correct core process. Supporting Evidence: PMID:1943992 Most reactions of this branched pathway are common to all organisms which are able to synthesize tryptophan, phenylalanine, and tyrosine. file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli |
| GO:0009423 chorismate biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: Derived from the YeastPathways ARO-PWY-1 ('chorismate biosynthesis') GO-CAM conversion. AROM catalyses steps 2-6 of chorismate biosynthesis; correct core process. Supporting Evidence: PMID:1943992 Most reactions of this branched pathway are common to all organisms which are able to synthesize tryptophan, phenylalanine, and tyrosine. file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli |
| GO:0009423 chorismate biosynthetic process | TAS PMID:1943992 Aromatic amino acid biosynthesis in the yeast Saccharomyces ... | ACCEPT | Summary: TAS annotation from PMID:1943992. The Braus review describes the gene-enzyme relationships of the yeast aromatic pathway, including AROM in the common chorismate trunk. Supporting Evidence: PMID:1943992 Most reactions of this branched pathway are common to all organisms which are able to synthesize tryptophan, phenylalanine, and tyrosine. file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic PMID:6355828 fragment also complemented aroA, aroB, aroD, and aroE mutants of Escherichia coli |
| GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups | IEA GO_REF:0000002 | MODIFY | Summary: IEA from InterPro2GO mapping (InterPro:IPR001986, InterPro:IPR036968). The alkyl/aryl-transferase grouping derives from the EPSP synthase domain (InterPro EPSP synthase family); the specific activity, 3-phosphoshikimate 1-carboxyvinyltransferase, is known and should be used. Proposed replacements: 3-phosphoshikimate 1-carboxyvinyltransferase activity Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt In the 2nd section; belongs to the EPSP synthase family. PMID:6355828 express 5 to 12 times the normal level of the five AROl enzyme activities |
| GO:0046394 carboxylic acid biosynthetic process | IEA GO_REF:0000117 | MODIFY | Summary: IEA from ARBA machine-learning rule (ARBA:ARBA00027883). Very general parent class; the specific process (chorismate biosynthesis) is known and already annotated. Proposed replacements: chorismate biosynthetic process Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic |
| GO:0046417 chorismate metabolic process | RCA GO_REF:0000123 | MODIFY | Summary: Derived from the YeastPathways ALL-CHORISMATE-PWY-1 ('superpathway of chorismate metabolism') GO-CAM conversion. Inherited from the chorismate superpathway; AROM does not act on chorismate itself but makes its precursor EPSP, so the biosynthetic child term is the accurate one. Proposed replacements: chorismate biosynthetic process Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic |
| GO:0046872 metal ion binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: IEA from UniRule-based electronic annotation (UniRule:UR000166141). AROM binds two Zn2+ per subunit (DHQ synthase domain metal); metal binding is a cofactor property, not a core function. The more specific zinc ion binding term is also present. Supporting Evidence: file:yeast/ARO1/ARO1-uniprot.txt Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- |
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Download this section (compressed HTML)Pentafunctional arom protein; catalyzes steps 2 through 6 in the biosynthesis of chorismate, which is a precursor to aromatic amino acids
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