C3L8S1 (C3L8S1_BACAC) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 32.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Histidinol-phosphate aminotransferase HAMAP-Rule MF_01023 EC=2.6.1.9 HAMAP-Rule MF_01023 Alternative name(s): Imidazole acetol-phosphate transaminase HAMAP-Rule MF_01023 | ||||||
| Gene names |
| ||||||
| Organism | Bacillus anthracis (strain CDC 684 / NRRL 3495) [Complete proteome] [HAMAP] EMBL ACP14923.1 | ||||||
| Taxonomic identifier | 568206 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 370 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP-Rule MF_01023 SAAS SAAS005861 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP-Rule MF_01023 SAAS SAAS005861 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP-Rule MF_01023 SAAS SAAS005861 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_01023 |
| Sequence similarities | Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. HAMAP-Rule MF_01023 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis HAMAP-Rule MF_01023 SAAS SAAS005861 |
| Ligand | Pyridoxal phosphate SAAS SAAS005861 HAMAP-Rule MF_01023 |
| Molecular function | Aminotransferase SAAS SAAS005861 HAMAP-Rule MF_01023 EMBL ACP14923.1 Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activityInferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Amino acid modifications | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Modified residue | 222 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01023 | ||||||
Sequences
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References
| [1] | "Genome sequence of Bacillus anthracis str. CDC 684." Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C., Sutton G., Sims D. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 684 / NRRL 3495. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001215 Genomic DNA. Translation: ACP14923.1. |
| RefSeq | YP_002815644.1. NC_012581.1. |
3D structure databases | |
| ProteinModelPortal | C3L8S1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 568206.BAMEG_3054. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACP14923; ACP14923; BAMEG_3054. |
| GeneID | 7787062. |
| KEGG | bah:BAMEG_3054. |
| PATRIC | 18795909. VBIBacAnt127120_3331. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0079. |
| HOGENOM | HOG000288510. |
| KO | K00817. |
| OMA | AASEIAC. |
| ProtClustDB | PRK03158. |
Enzyme and pathway databases | |
| BioCyc | BANT568206:GHVT-3016-MONOMER. |
| UniPathway | UPA00031; UER00012. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 1 hit. |
| HAMAP | MF_01023. HisC_aminotrans_2. |
| InterPro | IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR01141. hisC. 1 hit. |
| PROSITE | PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | C3L8S1_BACAC | ||||||||
| Accession | Primary (citable) accession number: C3L8S1 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
