O68602 (HIS4_CORGL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 97.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 Alternative name(s): Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase | ||||
| Gene names |
| ||||
| Organism | Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 196627 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › ![]() |
Protein attributes
| Sequence length | 246 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_01014 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the HisA/HisF family. |
| Caution | Ala-129 is present instead of the conserved Asp which is expected to be an active site residue. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP tryptophan biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylanthranilate isomerase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 246 | 246 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014 | PRO_0000142001 | |||||
Sites | |||||||||
| Active site | 10 | 1 | Proton acceptor By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 82 | 1 | G → S in AAC05575. Ref.1 | ||||||
| Sequence conflict | 90 – 92 | 3 | ERA → DTQ in AAC05575. Ref.1 | ||||||
| Sequence conflict | 105 | 1 | A → L in AAC05575. Ref.1 | ||||||
| Sequence conflict | 119 – 127 | 9 | RYGEKIAVD → AMARRLLS in AAC05575. Ref.1 | ||||||
| Sequence conflict | 157 | 1 | R → C in AAC05575. Ref.1 | ||||||
| Sequence conflict | 195 – 198 | 4 | PIVA → TYLT in AAC05575. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of the histidine biosynthetic genes of Corynebacterium glutamicum: organization and sequencing analysis of the hisA, impA, and hisF gene cluster." Jung S.-I., Han M.-S., Kwon J.-H., Cheon C.-I., Min K.-H., Lee M.-S. Biochem. Biophys. Res. Commun. 247:741-745(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613. |
| [2] | "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [3] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF051846 Genomic DNA. Translation: AAC05575.1. BA000036 Genomic DNA. Translation: BAB99489.1. BX927154 Genomic DNA. Translation: CAF20432.1. |
| PIR | JE0213. |
| RefSeq | NP_601295.1. NC_003450.3. YP_226333.1. NC_006958.1. |
3D structure databases | |
| ProteinModelPortal | O68602. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 196627.cg2299. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB99489; BAB99489; BAB99489. CAF20432; CAF20432; cg2299. |
| GeneID | 1020047. 3344802. |
| KEGG | cgb:cg2299. cgl:NCgl2015. |
| PATRIC | 21496192. VBICorGlu203724_2032. |
Phylogenomic databases | |
| eggNOG | COG0106. |
| HOGENOM | HOG000224614. |
| KO | K01814. |
| OMA | CARYVVT. |
| ProtClustDB | PRK14024. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627:GJDM-2069-MONOMER. |
| UniPathway | UPA00031; UER00009. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_01014. HisA. Divergent sequence. |
| InterPro | IPR013785. Aldolase_TIM. IPR006062. His_biosynth. IPR010188. HisA_TrpF. IPR023016. Isoase_HisA. IPR011060. RibuloseP-bd_barrel. [Graphical view] |
| Pfam | PF00977. His_biosynth. 1 hit. [Graphical view] |
| SUPFAM | SSF51366. RibP_bind_barrel. 1 hit. |
| TIGRFAMs | TIGR01919. hisA-trpF. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HIS4_CORGL | ||||||||
| Accession | Primary (citable) accession number: O68602 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
