Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbon monoxide dehydrogenase 2

Gene

cooS2

Organism
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).By similarity

Catalytic activityi

CO + H2O + A = CO2 + AH2.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inactivated by O2.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Iron-sulfur 1 (4Fe-4S); shared with dimeric partner
Metal bindingi47 – 471Iron-sulfur 1 (4Fe-4S); shared with dimeric partner
Metal bindingi48 – 481Iron-sulfur 2 (4Fe-4S)
Metal bindingi51 – 511Iron-sulfur 2 (4Fe-4S)
Metal bindingi56 – 561Iron-sulfur 2 (4Fe-4S)
Metal bindingi70 – 701Iron-sulfur 2 (4Fe-4S)
Metal bindingi261 – 2611Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen
Metal bindingi295 – 2951Nickel-iron-sulfur (Ni-4Fe-5S)
Metal bindingi333 – 3331Nickel-iron-sulfur (Ni-4Fe-5S)
Metal bindingi446 – 4461Nickel-iron-sulfur (Ni-4Fe-5S)
Metal bindingi476 – 4761Nickel-iron-sulfur (Ni-4Fe-5S)
Metal bindingi526 – 5261Nickel-iron-sulfur (Ni-4Fe-5S)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Nickel

Enzyme and pathway databases

BioCyciCHYD246194:GJCN-85-MONOMER.
BRENDAi1.2.99.2. 1178.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase 2 (EC:1.2.99.2)
Short name:
CODH 2
Gene namesi
Name:cooS2
Synonyms:cooSII
Ordered Locus Names:CHY_0085
OrganismiCarboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Taxonomic identifieri246194 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus
Proteomesi
  • UP000002706 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 636635Carbon monoxide dehydrogenase 2PRO_0000157138Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi246194.CHY_0085.

Structurei

Secondary structure

1
636
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73Combined sources
Helixi11 – 2313Combined sources
Helixi28 – 358Combined sources
Helixi40 – 445Combined sources
Beta strandi60 – 645Combined sources
Helixi74 – 10835Combined sources
Helixi120 – 13011Combined sources
Helixi139 – 15214Combined sources
Helixi162 – 1654Combined sources
Helixi170 – 1789Combined sources
Helixi186 – 19611Combined sources
Helixi205 – 23430Combined sources
Beta strandi240 – 2456Combined sources
Helixi246 – 2483Combined sources
Beta strandi253 – 2619Combined sources
Helixi263 – 27513Combined sources
Helixi277 – 2826Combined sources
Beta strandi288 – 2936Combined sources
Helixi294 – 30411Combined sources
Beta strandi308 – 3103Combined sources
Helixi312 – 3154Combined sources
Helixi316 – 3205Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi331 – 3333Combined sources
Helixi338 – 3458Combined sources
Beta strandi348 – 3514Combined sources
Beta strandi361 – 3633Combined sources
Helixi368 – 3703Combined sources
Helixi371 – 38818Combined sources
Turni389 – 3913Combined sources
Beta strandi401 – 4055Combined sources
Helixi409 – 4179Combined sources
Helixi425 – 4339Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi440 – 4434Combined sources
Helixi455 – 46612Combined sources
Beta strandi470 – 4745Combined sources
Helixi475 – 4839Combined sources
Turni484 – 4874Combined sources
Helixi489 – 4913Combined sources
Helixi492 – 4954Combined sources
Helixi498 – 51013Combined sources
Beta strandi513 – 5153Combined sources
Beta strandi519 – 5268Combined sources
Helixi529 – 54315Combined sources
Helixi547 – 5493Combined sources
Beta strandi550 – 5567Combined sources
Helixi562 – 57413Combined sources
Beta strandi577 – 5826Combined sources
Turni585 – 5884Combined sources
Helixi590 – 5978Combined sources
Turni598 – 6003Combined sources
Helixi601 – 6044Combined sources
Beta strandi607 – 6104Combined sources
Helixi614 – 63118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SU6X-ray1.64A1-636[»]
1SU7X-ray1.12A1-636[»]
1SU8X-ray1.10A1-636[»]
1SUFX-ray1.15A1-636[»]
2YIVX-ray1.28X1-636[»]
3B51X-ray1.40X4-636[»]
3B52X-ray1.50X4-636[»]
3B53X-ray1.50X4-636[»]
3I39X-ray1.36X1-636[»]
4UDXX-ray1.03X1-636[»]
4UDYX-ray1.09X1-636[»]
ProteinModelPortaliQ9F8A8.
SMRiQ9F8A8. Positions 4-636.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F8A8.

Family & Domainsi

Domaini

Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer.

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CJG. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000228918.
KOiK00198.
OMAiGCASHAQ.
OrthoDBiEOG6RNQ8R.

Family and domain databases

Gene3Di1.20.1270.30. 1 hit.
3.40.50.2030. 2 hits.
InterProiIPR016101. CO_DH_a-bundle.
IPR010047. CODH.
IPR004137. HCP/CODH.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamiPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFiPIRSF005023. CODH. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01702. CO_DH_cata. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9F8A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKQNLKSTD RAVQQMLDKA KREGIQTVWD RYEAMKPQCG FGETGLCCRH
60 70 80 90 100
CLQGPCRINP FGDEPKVGIC GATAEVIVAR GLDRSIAAGA AGHSGHAKHL
110 120 130 140 150
AHTLKKAVQG KAASYMIKDR TKLHSIAKRL GIPTEGQKDE DIALEVAKAA
160 170 180 190 200
LADFHEKDTP VLWVTTVLPP SRVKVLSAHG LIPAGIDHEI AEIMHRTSMG
210 220 230 240 250
CDADAQNLLL GGLRCSLADL AGCYMGTDLA DILFGTPAPV VTESNLGVLK
260 270 280 290 300
ADAVNVAVHG HNPVLSDIIV SVSKEMENEA RAAGATGINV VGICCTGNEV
310 320 330 340 350
LMRHGIPACT HSVSQEMAMI TGALDAMILD YQCIQPSVAT IAECTGTTVI
360 370 380 390 400
TTMEMSKITG ATHVNFAEEA AVENAKQILR LAIDTFKRRK GKPVEIPNIK
410 420 430 440 450
TKVVAGFSTE AIINALSKLN ANDPLKPLID NVVNGNIRGV CLFAGCNNVK
460 470 480 490 500
VPQDQNFTTI ARKLLKQNVL VVATGCGAGA LMRHGFMDPA NVDELCGDGL
510 520 530 540 550
KAVLTAIGEA NGLGGPLPPV LHMGSCVDNS RAVALVAALA NRLGVDLDRL
560 570 580 590 600
PVVASAAEAM HEKAVAIGTW AVTIGLPTHI GVLPPITGSL PVTQILTSSV
610 620 630
KDITGGYFIV ELDPETAADK LLAAINERRA GLGLPW
Length:636
Mass (Da):66,914
Last modified:January 23, 2007 - v4
Checksum:i61C1011E86022A63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti528 – 5281D → H in AAG29809 (PubMed:11024270).Curated
Sequence conflicti532 – 5321A → S in AAG29809 (PubMed:11024270).Curated
Sequence conflicti544 – 5441G → W in AAG29809 (PubMed:11024270).Curated
Sequence conflicti547 – 5471L → M in AAG29809 (PubMed:11024270).Curated
Sequence conflicti558 – 5581E → Q in AAG29809 (PubMed:11024270).Curated
Sequence conflicti583 – 5831L → F in AAG29809 (PubMed:11024270).Curated
Sequence conflicti615 – 6173ETA → VQQR in AAG29809 (PubMed:11024270).Curated
Sequence conflicti636 – 6361W → R in AAG29809 (PubMed:11024270).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249899 Genomic DNA. Translation: AAG29809.1.
CP000141 Genomic DNA. Translation: ABB15588.1.
AF244619 Genomic DNA. Translation: AAG23568.1.
RefSeqiWP_011343033.1. NC_007503.1.

Genome annotation databases

EnsemblBacteriaiABB15588; ABB15588; CHY_0085.
KEGGichy:CHY_0085.
PATRICi21273367. VBICarHyd26463_0083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249899 Genomic DNA. Translation: AAG29809.1.
CP000141 Genomic DNA. Translation: ABB15588.1.
AF244619 Genomic DNA. Translation: AAG23568.1.
RefSeqiWP_011343033.1. NC_007503.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SU6X-ray1.64A1-636[»]
1SU7X-ray1.12A1-636[»]
1SU8X-ray1.10A1-636[»]
1SUFX-ray1.15A1-636[»]
2YIVX-ray1.28X1-636[»]
3B51X-ray1.40X4-636[»]
3B52X-ray1.50X4-636[»]
3B53X-ray1.50X4-636[»]
3I39X-ray1.36X1-636[»]
4UDXX-ray1.03X1-636[»]
4UDYX-ray1.09X1-636[»]
ProteinModelPortaliQ9F8A8.
SMRiQ9F8A8. Positions 4-636.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246194.CHY_0085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB15588; ABB15588; CHY_0085.
KEGGichy:CHY_0085.
PATRICi21273367. VBICarHyd26463_0083.

Phylogenomic databases

eggNOGiENOG4105CJG. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000228918.
KOiK00198.
OMAiGCASHAQ.
OrthoDBiEOG6RNQ8R.

Enzyme and pathway databases

BioCyciCHYD246194:GJCN-85-MONOMER.
BRENDAi1.2.99.2. 1178.

Miscellaneous databases

EvolutionaryTraceiQ9F8A8.

Family and domain databases

Gene3Di1.20.1270.30. 1 hit.
3.40.50.2030. 2 hits.
InterProiIPR016101. CO_DH_a-bundle.
IPR010047. CODH.
IPR004137. HCP/CODH.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamiPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFiPIRSF005023. CODH. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01702. CO_DH_cata. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide dehydrogenase genes cooF and cooS."
    Gonzalez J.M., Robb F.T.
    FEMS Microbiol. Lett. 191:243-247(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-161 / DSM 6008 / Z-2901.
  3. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION.
  4. "A genomic survey of the extreme thermophilic, CO-utilizing bacterium Carboxydothermus hydrogenoformans."
    Gonzalez J.M., Robb F.T.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-429.
  5. "Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster."
    Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O.
    Science 293:1281-1285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiCOOS2_CARHZ
AccessioniPrimary (citable) accession number: Q9F8A8
Secondary accession number(s): Q3AFX7, Q9F8L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.