P59934 (COOS1_CARHZ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
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: Carbon monoxide dehydrogenase 1 Short name=CODH 1 EC=1.2.99.2 | ||||
| Gene names |
| ||||
| Organism | Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 246194 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Carboxydothermus |
Protein attributes
| Sequence length | 636 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) By similarity. |
| Catalytic activity | CO + H2O + A = CO2 + AH2. |
| Cofactor | Binds 3 4Fe-4S clusters per homodimer By similarity. Binds 2 nickel-iron-sulfur clusters per homodimer By similarity. |
| Enzyme regulation | Inactivated by O2. |
| Subunit structure | Homodimer. |
| Subcellular location | Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Loosely attached to the membrane, probably via CooF. Ref.2 |
| Sequence similarities | Belongs to the Ni-containing carbon monoxide dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Cytoplasm Membrane |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding Nickel |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | generation of precursor metabolites and energy Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activityInferred from electronic annotation. Source: EC nickel cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 636 | 635 | Carbon monoxide dehydrogenase 1 | PRO_0000157137 | |||||
Sites | |||||||||
| Metal binding | 38 | 1 | Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity | ||||||
| Metal binding | 46 | 1 | Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity | ||||||
| Metal binding | 47 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 50 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 55 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 69 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 262 | 1 | Nickel-iron-sulfur By similarity | ||||||
| Metal binding | 297 | 1 | Nickel-iron-sulfur By similarity | ||||||
| Metal binding | 335 | 1 | Nickel-iron-sulfur By similarity | ||||||
| Metal binding | 448 | 1 | Nickel-iron-sulfur By similarity | ||||||
| Metal binding | 478 | 1 | Nickel-iron-sulfur By similarity | ||||||
| Metal binding | 528 | 1 | Nickel-iron-sulfur By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 10 | 1 | P → D AA sequence Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901." Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A. PLoS Genet. 1:563-574(2005) [PubMed: 16311624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Z-2901 / DSM 6008. |
| [2] | "Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans." Svetlitchnyi V., Peschel C., Acker G., Meyer O. J. Bacteriol. 183:5134-5144(2001) [PubMed: 11489867] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-23, SUBCELLULAR LOCATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000141 Genomic DNA. Translation: ABB14432.1. |
| RefSeq | YP_360644.1. NC_007503.1. |
3D structure databases | |
| ProteinModelPortal | P59934. |
| SMR | P59934. Positions 25-634. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P59934. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3728783. |
| GenomeReviews | Gene locus CHY_1824 in contig CP000141_GR. |
| KEGG | chy:CHY_1824. |
| NMPDR | fig|246194.3.peg.2363. |
| PATRIC | 21276751. VBICarHyd26463_1739. |
| TIGR | CHY_1824. |
Phylogenomic databases | |
| eggNOG | COG1151. |
| HOGENOM | HBG393174. |
| OMA | HGRHIAL. |
| ProtClustDB | CLSK862738. |
Enzyme and pathway databases | |
| BioCyc | CHYD246194:CHY_1824-MONOMER. |
Family and domain databases | |
| InterPro | IPR016101. CO_DH_a-bundle. IPR010047. CO_DH_cat. IPR004137. Prismane. IPR011254. Prismane-like. IPR016099. Prismane-like_a/b-sand. [Graphical view] |
| Gene3D | G3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit. G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 2 hits. |
| KO | K00190. |
| Pfam | PF03063. Prismane. 1 hit. [Graphical view] |
| PIRSF | PIRSF005023. CODH. 1 hit. |
| SUPFAM | SSF56821. Prismane_like. 1 hit. |
| TIGRFAMs | TIGR01702. CO_DH_cata. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | COOS1_CARHZ | ||||||||
| Accession | Primary (citable) accession number: P59934 Secondary accession number(s): Q3AB40 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with