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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).1 Publication

Catalytic activityi

CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+.3 Publications

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inactivated by O2.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi39Iron-sulfur 1 (4Fe-4S); shared with dimeric partner1 Publication1
Metal bindingi47Iron-sulfur 1 (4Fe-4S); shared with dimeric partner1 Publication1
Metal bindingi48Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi51Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi56Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi70Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi261Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen3 Publications1
Metal bindingi295Nickel-iron-sulfur (Ni-4Fe-5S)3 Publications1
Metal bindingi333Nickel-iron-sulfur (Ni-4Fe-5S)3 Publications1
Metal bindingi446Nickel-iron-sulfur (Ni-4Fe-5S)3 Publications1
Metal bindingi476Nickel-iron-sulfur (Ni-4Fe-5S)3 Publications1
Metal bindingi526Nickel-iron-sulfur (Ni-4Fe-5S)3 Publications1

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

BRENDAi1.2.99.2. 1178.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase 2 (EC:1.2.7.43 Publications)
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

  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

  • Note: Loosely attached to the membrane, probably via CooF.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001571382 – 636Carbon monoxide dehydrogenase 2Add BLAST635

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi246194.CHY_0085.

Structurei

Secondary structure

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 7Combined sources3
Helixi11 – 23Combined sources13
Helixi28 – 35Combined sources8
Helixi40 – 44Combined sources5
Beta strandi60 – 64Combined sources5
Helixi74 – 108Combined sources35
Helixi120 – 130Combined sources11
Helixi139 – 152Combined sources14
Helixi162 – 165Combined sources4
Helixi170 – 178Combined sources9
Helixi186 – 196Combined sources11
Helixi205 – 234Combined sources30
Beta strandi240 – 245Combined sources6
Helixi246 – 248Combined sources3
Beta strandi253 – 261Combined sources9
Helixi263 – 275Combined sources13
Helixi277 – 282Combined sources6
Beta strandi288 – 293Combined sources6
Helixi294 – 304Combined sources11
Beta strandi308 – 310Combined sources3
Helixi312 – 315Combined sources4
Helixi316 – 320Combined sources5
Beta strandi324 – 329Combined sources6
Beta strandi331 – 333Combined sources3
Helixi338 – 345Combined sources8
Beta strandi348 – 351Combined sources4
Beta strandi361 – 363Combined sources3
Helixi368 – 370Combined sources3
Helixi371 – 388Combined sources18
Turni389 – 391Combined sources3
Beta strandi401 – 405Combined sources5
Helixi409 – 417Combined sources9
Helixi425 – 433Combined sources9
Beta strandi435 – 437Combined sources3
Beta strandi440 – 443Combined sources4
Helixi455 – 466Combined sources12
Beta strandi470 – 474Combined sources5
Helixi475 – 483Combined sources9
Turni484 – 487Combined sources4
Helixi489 – 491Combined sources3
Helixi492 – 495Combined sources4
Helixi498 – 510Combined sources13
Beta strandi513 – 515Combined sources3
Beta strandi519 – 526Combined sources8
Helixi529 – 543Combined sources15
Helixi547 – 549Combined sources3
Beta strandi550 – 556Combined sources7
Helixi562 – 574Combined sources13
Beta strandi577 – 582Combined sources6
Turni585 – 588Combined sources4
Helixi590 – 597Combined sources8
Turni598 – 600Combined sources3
Helixi601 – 604Combined sources4
Beta strandi607 – 610Combined sources4
Helixi614 – 631Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FLEX-ray1.23X4-636[»]
ProteinModelPortaliQ9F8A8.
SMRiQ9F8A8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F8A8.

Family & Domainsi

Domaini

Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.3 Publications

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CJG. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000228918.
KOiK00198.
OMAiGCASHAQ.
OrthoDBiPOG091H103J.

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)DescriptionActionsGraphical viewLength
Sequence conflicti528D → H in AAG29809 (PubMed:11024270).Curated1
Sequence conflicti532A → S in AAG29809 (PubMed:11024270).Curated1
Sequence conflicti544G → W in AAG29809 (PubMed:11024270).Curated1
Sequence conflicti547L → M in AAG29809 (PubMed:11024270).Curated1
Sequence conflicti558E → Q in AAG29809 (PubMed:11024270).Curated1
Sequence conflicti583L → F in AAG29809 (PubMed:11024270).Curated1
Sequence conflicti615 – 617ETA → VQQR in AAG29809 (PubMed:11024270).Curated3
Sequence conflicti636W → R in AAG29809 (PubMed:11024270).Curated1

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
PDB 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[»]
5FLEX-ray1.23X4-636[»]
ProteinModelPortaliQ9F8A8.
SMRiQ9F8A8.
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.
OrthoDBiPOG091H103J.

Enzyme and pathway databases

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...

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: November 30, 2016
This is version 112 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.