A3CWS8 (HIS8_METMJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 46.
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: Histidinol-phosphate aminotransferase EC=2.6.1.9 Alternative name(s): Imidazole acetol-phosphate transaminase | ||||
| Gene names |
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| Organism | Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 368407 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Methanomicrobiaceae › Methanoculleus › ![]() |
Protein attributes
| Sequence length | 352 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 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP-Rule MF_01023 |
| Sequence similarities | Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 352 | 352 | Histidinol-phosphate aminotransferase HAMAP-Rule MF_01023 | PRO_0000319801 | |||||
Amino acid modifications | |||||||||
| Modified residue | 216 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1." Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. Kyrpides N.C.Stand. Genomic Sci. 1:189-196(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35101 / DSM 1498 / JR1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000562 Genomic DNA. Translation: ABN57828.1. |
| RefSeq | YP_001047810.1. NC_009051.1. |
3D structure databases | |
| ProteinModelPortal | A3CWS8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 368407.Memar_1902. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABN57828; ABN57828; Memar_1902. |
| GeneID | 4846352. |
| KEGG | mem:Memar_1902. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0079. |
| HOGENOM | HOG000288510. |
| KO | K00817. |
| OMA | VGRTMSK. |
| ProtClustDB | PRK00950. |
Enzyme and pathway databases | |
| BioCyc | MMAR368407:GH7L-1955-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 | 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS8_METMJ | ||||||||
| Accession | Primary (citable) accession number: A3CWS8 | ||||||||
| 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
