Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB record A0A0H2M8T9 (A0A0H2M8T9_VARPD) - Ferric uptake regulation protein Fur1 from Variovorax paradoxus TBEA6
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VPARA_18200 (fur1, A0A0H2M8T9) is a 139-aa Fur-family ferric uptake regulator (NCBIfam NF006999, Pfam PF01475, InterPro IPR002481, PANTHER PTHR33202:SF2) containing a regulatory Fe(2+)/Mn(2+)-binding site (His86, Asp88, Glu107, His124; PIRSR PIRSR602481-2) and a four-cysteine structural Zn(2+)-binding site (Cys92, Cys95, Cys132, Cys135; PIRSR PIRSR602481-1).
"CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR602481-2};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR602481-2};
CC Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR602481-2};"
Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: purification and activity on iron-regulated promoters.
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Purified Fur-Fe(II) specifically binds conserved 19-bp Fur-box operator sequences overlapping iron-regulated siderophore pathway promoters to repress transcription under iron-replete conditions.
"The DNA binding activity of the PA-Fur protein was confirmed by gel mobility shift assays and DNase I footprints of the synthetic DNA fragment GATAAT GATAATCATTATC, representing a perfect "Fur box"."
Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator.
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X-ray crystallography and X-ray absorption spectroscopy establish that Fur possesses distinct structural Zn(2+) and regulatory Fe(2+) binding sites per monomer.
"Here, we present the first crystal structure of Fur from P. aeruginosa in complex with Zn2+ determined at a resolution of 1.8 A. Furthermore, X-ray absorption spectroscopic measurements and microPIXE analysis were performed in order to characterize the distinct zinc and iron binding sites in solution."
An automated Genomes-to-Natural Products platform (GNP) for the discovery of modular natural products.
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Demonstrates that Variovorax paradoxus biosynthesizes vacidobactin A/B and variobactin A/B siderophores.
"Isolation of these indicated metabolites provided the novel compounds vacidobactin A and B, which are methylmalonate-incorporating acidobactins and represent the first natural products isolated from Variovorax"