P45358 (HIS8_ACEPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 63.
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 | Acetobacter pasteurianus (Acetobacter turbidans) | ||||
| Taxonomic identifier | 438 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acetobacter |
Protein attributes
| Sequence length | 356 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 MF_01023 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_01023 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 |
| Subunit structure | Homodimer By similarity. HAMAP 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 |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activityInferred from electronic annotation. Source: EC 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 – 356 | 356 | Histidinol-phosphate aminotransferase HAMAP MF_01023 | PRO_0000153290 | |||||
Amino acid modifications | |||||||||
| Modified residue | 210 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Suppression of an ethanol-sensitive mutation of Acetobacter pasteurianus by overexpression of the his1 gene encoding histidinol phosphate aminotransferase." Takemura H., Horinouchi S., Beppu T. J. Ferment. Bioeng. 76:224-228(1993) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCI 1452. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D14440 Genomic DNA. Translation: BAA03332.1. |
| PIR | I39488. |
3D structure databases | |
| ProteinModelPortal | P45358. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_01023. HisC_aminotrans_2. [Tree] |
| InterPro | IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| 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 | HIS8_ACEPA | ||||||||
| Accession | Primary (citable) accession number: P45358 | ||||||||
| 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 |

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