Q3V8A3 (PDXA_METCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 52.
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: 4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 Alternative name(s): 4-(phosphohydroxy)-L-threonine dehydrogenase | ||||
| Gene names |
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| Organism | Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243233 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus › ![]() |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) By similarity. HAMAP-Rule MF_00536 |
| Catalytic activity | 4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule MF_00536 |
| Cofactor | Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt By similarity. |
| Pathway | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_00536 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00536. |
| Miscellaneous | The active site is located at the dimer interface By similarity. HAMAP-Rule MF_00536 |
| Sequence similarities | Belongs to the PdxA family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridoxine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Cobalt Magnesium Metal-binding NAD NADP Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 4-hydroxythreonine-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP NAD bindingInferred from electronic annotation. Source: InterPro cobalt ion bindingInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 330 | 330 | 4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536 | PRO_1000081868 | |||||
Sites | |||||||||
| Metal binding | 163 | 1 | Divalent metal cation; shared with dimeric partner By similarity | ||||||
| Metal binding | 208 | 1 | Divalent metal cation; shared with dimeric partner By similarity | ||||||
| Metal binding | 263 | 1 | Divalent metal cation; shared with dimeric partner By similarity | ||||||
| Binding site | 134 | 1 | Substrate By similarity | ||||||
| Binding site | 135 | 1 | Substrate By similarity | ||||||
| Binding site | 271 | 1 | Substrate By similarity | ||||||
| Binding site | 280 | 1 | Substrate By similarity | ||||||
| Binding site | 289 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. Eisen J.A.PLoS Biol. 2:1616-1628(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33009 / NCIMB 11132 / Bath. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017282 Genomic DNA. Translation: AAU93126.1. |
| RefSeq | YP_113119.1. NC_002977.6. |
3D structure databases | |
| ProteinModelPortal | Q3V8A3. |
| SMR | Q3V8A3. Positions 1-325. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243233.MCA0603. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAU93126; AAU93126; MCA0603. |
| GeneID | 3103080. |
| KEGG | mca:MCA0603. |
| PATRIC | 22604976. VBIMetCap22254_0620. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1995. |
| HOGENOM | HOG000221592. |
| KO | K00097. |
| OMA | HFAGMIT. |
Enzyme and pathway databases | |
| UniPathway | UPA00244; UER00312. |
Family and domain databases | |
| Gene3D | 3.40.718.10. 1 hit. |
| HAMAP | MF_00536. PdxA. |
| InterPro | IPR024084. IsoPropMal-DH-like_dom. IPR005255. PdxA. [Graphical view] |
| Pfam | PF04166. PdxA. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00557. pdxA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PDXA_METCA | ||||||||
| Accession | Primary (citable) accession number: Q3V8A3 | ||||||||
| 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
