Reviewed,
UniProtKB/Swiss-Prot Q81SV5 (HIS81_BACAN)
Last modified
February 9, 2010.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histidinol-phosphate aminotransferase 1 EC=2.6.1.9 Alternative name(s): Imidazole acetol-phosphate transaminase 1 | ||||||
| Gene names |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1392 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › 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 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 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | histidinol-phosphate transaminase activity Inferred 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 – 370 | 370 | Histidinol-phosphate aminotransferase 1 HAMAP MF_01023 | PRO_0000153297 | |||||
Amino acid modifications | |||||||||
| Modified residue | 222 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP25476.1. AE017334 Genomic DNA. Translation: AAT30637.1. AE017225 Genomic DNA. Translation: AAT53748.1. |
| RefSeq | NP_843990.1. YP_018162.1. YP_027697.1. |
3D structure databases | |
| SMR | Q81SV5. Positions 4-358. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1087402. 2817576. 2849454. |
| GenomeReviews | Gene locus BA_1539 in contig AE016879_GR. Gene locus BAS1428 in contig AE017225_GR. Gene locus GBAA_1539 in contig AE017334_GR. |
| KEGG | ban:BA1539. bar:GBAA1539. bat:BAS1428. |
| TIGR | BA_1539. GBAA_1539. |
Phylogenomic databases | |
| HOGENOM | HBG646350. |
| OMA | KGYIVRS. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS1428-MONOMER. BANT261594:GBAA1539-MONOMER. |
| BRENDA | 2.6.1.9. 267517. |
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. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01141. hisC. 1 hit. |
| PROSITE | PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS81_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81SV5 Secondary accession number(s): Q6I134, Q6KUY8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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