Reviewed,
UniProtKB/Swiss-Prot Q3SI68 (HIS82_THIDA)
Last modified
November 3, 2009.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Histidinol-phosphate aminotransferase 2 EC=2.6.1.9 Alternative name(s): Imidazole acetol-phosphate transaminase 2 | ||||
| Gene names |
| ||||
| Organism | Thiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 292415 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Hydrogenophilales › Hydrogenophilaceae › Thiobacillus |
Protein attributes
| Sequence length | 357 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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. |
| 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 – 357 | 357 | Histidinol-phosphate aminotransferase 2 HAMAP MF_01023 | PRO_0000153472 | |||||
Amino acid modifications | |||||||||
| Modified residue | 215 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans." Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P. J. Bacteriol. 188:1473-1488(2006) [PubMed: 16452431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000116 Genomic DNA. Translation: AAZ97665.1. | |
| RefSeq | YP_315470.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3SI68. |
Genome annotation databases | |
| GeneID | 3671295. |
| GenomeReviews | Gene locus Tbd_1712 in contig CP000116_GR. |
| KEGG | tbd:Tbd_1712. |
| NMPDR | fig|292415.3.peg.1809. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q3SI68. |
| OMA | DEQFQIR. |
Enzyme and pathway databases | |
| BioCyc | TDEN292415:TBD_1712-MON. |
Family and domain databases | |
| HAMAP | MF_01023. [Tree] |
| InterPro | IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS82_THIDA | ||||||||
| Accession | Primary (citable) accession number: Q3SI68 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with


