HIS5

UniProt ID: P07172
Organism: Saccharomyces cerevisiae S288C
Review Status: DRAFT
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Gene Description

Histidinol-phosphate aminotransferase (EC 2.6.1.9) of Saccharomyces cerevisiae, the HisC orthologue and a class II (fold type I) pyridoxal 5'-phosphate-dependent aminotransferase. It catalyses step 7 of L-histidine biosynthesis, the reversible transamination of imidazole-acetol phosphate with L-glutamate to give L-histidinol phosphate and 2-oxoglutarate. It is a cytosolic enzyme and its gene is under GCN4 general amino acid control. Bacterial HisC enzymes can transaminate aromatic amino acids in vitro, but in yeast the aromatic aminotransferases Aro8 and Aro9 account for phenylalanine and tyrosine transamination, since aro8 aro9 double mutants are Phe/Tyr auxotrophs despite an intact HIS5.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000105 L-histidine biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: Electronic annotation (InterPro/UniPathway/ARBA) consistent with the enzyme's catalytic step in histidine biosynthesis. HIS5 catalyses step 7, histidinol-phosphate aminotransferase of the pathway, so this is the core biological process.
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
GO:0000105 L-histidine biosynthetic process
IMP
PMID:14190241
GENE-ENZYME RELATIONS IN HISTIDINE BIOSYNTHESIS IN YEAST.
ACCEPT
Summary: Mutant phenotype (histidine auxotrophy with loss of the corresponding enzymatic step) directly ties the gene product to histidine biosynthesis. HIS5 catalyses step 7, histidinol-phosphate aminotransferase of the pathway, so this is the core biological process.
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
GO:0000105 L-histidine biosynthetic process
RCA
GO_REF:0000123
ACCEPT
Summary: Derived from YeastPathways HISTSYN-PWY (L-histidine biosynthesis), in which this gene catalyses a defined step. HIS5 catalyses step 7, histidinol-phosphate aminotransferase of the pathway, so this is the core biological process.
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
GO:0004400 L-histidinol-phosphate:2-oxoglutarate transaminase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Electronic annotation from InterPro/Rhea/EC mapping; consistent with domain architecture and experimental data. This is the core catalytic activity of HIS5 (step 7, histidinol-phosphate aminotransferase).
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
GO:0004400 L-histidinol-phosphate:2-oxoglutarate transaminase activity
IMP
PMID:14190241
GENE-ENZYME RELATIONS IN HISTIDINE BIOSYNTHESIS IN YEAST.
ACCEPT
Summary: Mutants in this gene lack the corresponding enzymatic step (Fink 1964 gene-enzyme correlation). This is the core catalytic activity of HIS5 (step 7, histidinol-phosphate aminotransferase).
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
GO:0004400 L-histidinol-phosphate:2-oxoglutarate transaminase activity
RCA
GO_REF:0000123
ACCEPT
Summary: YeastPathways (ALL-CHORISMATE-PWY-1) assignment of this reaction to HIS5; MF correct irrespective of which pathway diagram generated the row. This is the core catalytic activity of HIS5 (step 7, histidinol-phosphate aminotransferase).
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
GO:0004400 L-histidinol-phosphate:2-oxoglutarate transaminase activity
RCA
GO_REF:0000123
ACCEPT
Summary: YeastPathways (HISTSYN-PWY) assignment of this reaction to HIS5; MF correct irrespective of which pathway diagram generated the row. This is the core catalytic activity of HIS5 (step 7, histidinol-phosphate aminotransferase).
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
GO:0004400 L-histidinol-phosphate:2-oxoglutarate transaminase activity
RCA
GO_REF:0000123
ACCEPT
Summary: YeastPathways (PRPP-PWY-1) assignment of this reaction to HIS5; MF correct irrespective of which pathway diagram generated the row. This is the core catalytic activity of HIS5 (step 7, histidinol-phosphate aminotransferase).
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
GO:0005737 cytoplasm
HDA
PMID:14562095
Global analysis of protein localization in budding yeast.
ACCEPT
Summary: High-throughput GFP-fusion localisation (Huh et al. 2003) placed the protein in the cytoplasm. Consistent with a soluble cytosolic biosynthetic enzyme.
Supporting Evidence:
PMID:14562095
We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories
GO:0005829 cytosol
RCA
GO_REF:0000123
ACCEPT
Summary: RCA from YeastPathways (ALL-CHORISMATE-PWY-1). The histidine biosynthetic enzymes of S. cerevisiae are soluble cytosolic proteins with no targeting signals, so is_active_in cytosol is correct regardless of which pathway diagram generated the row.
Supporting Evidence:
PMID:14562095
We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories
GO:0005829 cytosol
RCA
GO_REF:0000123
ACCEPT
Summary: RCA from YeastPathways (HISTSYN-PWY). The histidine biosynthetic enzymes of S. cerevisiae are soluble cytosolic proteins with no targeting signals, so is_active_in cytosol is correct regardless of which pathway diagram generated the row.
Supporting Evidence:
PMID:14562095
We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories
GO:0005829 cytosol
RCA
GO_REF:0000123
ACCEPT
Summary: RCA from YeastPathways (PRPP-PWY-1). The histidine biosynthetic enzymes of S. cerevisiae are soluble cytosolic proteins with no targeting signals, so is_active_in cytosol is correct regardless of which pathway diagram generated the row.
Supporting Evidence:
PMID:14562095
We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories
GO:0005829 cytosol
RCA
GO_REF:0000123
ACCEPT
Summary: RCA from YeastPathways (PWY3O-4115). The histidine biosynthetic enzymes of S. cerevisiae are soluble cytosolic proteins with no targeting signals, so is_active_in cytosol is correct regardless of which pathway diagram generated the row.
Supporting Evidence:
PMID:14562095
We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories
GO:0006559 L-phenylalanine catabolic process
RCA
GO_REF:0000123
REMOVE
Summary: RCA from YeastPathways PWY3O-4115. Phenylalanine catabolism (Ehrlich pathway) transamination in yeast is attributed to Aro8/Aro9; there is no experimental evidence that His5 contributes, and its demonstrated role is histidine biosynthesis. The pathway-database inclusion appears to be by analogy to bacterial HisC promiscuity and is not supported for the yeast enzyme.
Supporting Evidence:
PMID:9491082
aro8 and aro9 double mutants which are auxotrophic for both phenylalanine and tyrosine
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
GO:0008793 aromatic-amino-acid:2-oxoglutarate transaminase activity
RCA
GO_REF:0000123
MARK AS OVER ANNOTATED
Summary: RCA from YeastPathways PWY3O-4115 (phenylalanine degradation/Ehrlich pathway transamination), which lists HIS5 alongside the aromatic aminotransferases Aro8/Aro9, presumably by analogy to the substrate promiscuity of bacterial HisC. No yeast experiment shows His5 transaminating aromatic amino acids, and aro8 aro9 double mutants are phenylalanine/tyrosine auxotrophs, indicating His5 cannot substitute in vivo. A minor in vitro side activity cannot be excluded, so marked as over-annotation rather than removed.
Supporting Evidence:
PMID:9491082
aro8 and aro9 double mutants which are auxotrophic for both phenylalanine and tyrosine
GO:0009165 nucleotide biosynthetic process
RCA
GO_REF:0000123
REMOVE
Summary: RCA propagated from the YeastPathways superpathway PRPP-PWY-1 (superpathway of histidine, purine and pyrimidine biosynthesis), which assigns the umbrella process to every member enzyme. HIS5 catalyses step 7, histidinol-phosphate aminotransferase of L-histidine biosynthesis; its substrates and products are histidine-pathway intermediates, and it performs no step of nucleotide biosynthesis. Sharing PRPP as a precursor with nucleotide synthesis is not participation. The pathway-bundling artefact should be removed.
Supporting Evidence:
PMID:14190241
Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
GO:0016740 transferase activity
IEA
GO_REF:0000002
MODIFY
Summary: Generic electronic annotation (transferase activity); the specific activity is L-histidinol-phosphate:2-oxoglutarate transaminase (GO:0004400). Note that histidinol phosphate is not an amino acid, so the amino-acid-transaminase grouping is also imprecise.
Supporting Evidence:
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
GO:0030170 pyridoxal phosphate binding
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: PLP is the cofactor of this class II aminotransferase; correct cofactor-binding annotation but non-core.
Supporting Evidence:
file:yeast/HIS5/HIS5-uniprot.txt
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
GO:0046417 chorismate metabolic process
RCA
GO_REF:0000123
REMOVE
Summary: RCA from the YeastPathways superpathway ALL-CHORISMATE-PWY-1 (superpathway of chorismate metabolism), which bundles aromatic amino acid branches. His5 neither produces nor consumes chorismate, and its inclusion rests on a putative aromatic aminotransferase side activity not supported in yeast.
Supporting Evidence:
PMID:9491082
aro8 and aro9 double mutants which are auxotrophic for both phenylalanine and tyrosine
GO:0140385 amino acid transaminase activity
IEA
GO_REF:0000117
MODIFY
Summary: Generic electronic annotation (amino acid transaminase activity); the specific activity is L-histidinol-phosphate:2-oxoglutarate transaminase (GO:0004400). Note that histidinol phosphate is not an amino acid, so the amino-acid-transaminase grouping is also imprecise.
Supporting Evidence:
file:yeast/HIS5/HIS5-uniprot.txt
RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};

Core Functions

Catalyses step 7 of L-histidine biosynthesis, the PLP-dependent transamination between imidazole-acetol phosphate and L-glutamate yielding L-histidinol phosphate (EC 2.6.1.9).

Supporting Evidence:
  • PMID:14190241
    Each of the histidine mutants of Saccharomyces cerevisiae has been correlated with a particular step in histidine biosynthesis
  • file:yeast/HIS5/HIS5-uniprot.txt
    RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};

References

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Deep Research

SGD

(HIS5-deep-research-sgd.md)
SGD gene description for HIS5 (yeast) SGD

SGD gene description for HIS5 (yeast)

Histidinol-phosphate aminotransferase; catalyzes the seventh step in histidine biosynthesis; responsive to general control of amino acid biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts

πŸ“š Additional Documentation

Notes

(HIS5-notes.md)

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