[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1748656 [NCBI, ExPASy, EBI, Israel, Japan] Morton T.A., Runquist J.A., Ragsdale S.W., Shanmugasundaram T., Wood H.G., Ljungdahl L.G.; "The primary structure of the subunits of carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum."; J. Biol. Chem. 266:23824-23828(1991).
[2]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1126/science.1075843; PubMed=12386327 [NCBI, ExPASy, EBI, Israel, Japan] Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L.; "A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase."; Science 298:567-572(2002).
[3]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1038/nsb912; PubMed=12627225 [NCBI, ExPASy, EBI, Israel, Japan] Darnault C., Volbeda A., Kim E.J., Legrand P., Vernede X., Lindahl P.A., Fontecilla-Camps J.-C.; "Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase."; Nat. Struct. Biol. 10:271-279(2003).

Comments

FUNCTION: The beta subunit (this protein) generates CO from CO(2), while the alpha subunit combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur protein.
CATALYTIC ACTIVITY: CO + H₂O + 2 oxidized ferredoxin = CO₂ + 2 reduced ferredoxin + 2 H⁺.
CATALYTIC ACTIVITY: CO + H₂O + A = CO₂ + AH₂.
COFACTOR: Binds 1 nickel-iron-sulfur cluster per subunit.
COFACTOR: Binds 2 4Fe-4S clusters per homodimer.
SUBUNIT: Tetramer of two alpha and two beta chains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M62727; AAA23228.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41670; A41670.

3D structure databases

PDB

1MJG; X-ray; 2.20 A; A/B/C/D=1-674.	[ExPASy / RCSB / EBI]
1OAO; X-ray; 1.90 A; A/B=1-674.	[ExPASy / RCSB / EBI]
2Z8Y; X-ray; 2.51 A; A/B/C/D=1-674.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MJG; -.
1OAO; -.
2Z8Y; -.

ModBase

P27989.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0018492;	Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from InterPro).
GO:0043885;	Molecular function: carbon-monoxide dehydrogenase (ferredoxin) activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151;	Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0015977;	Biological process: carbon utilization by fixation of carbon dioxide (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002110; ANK.
IPR016101; CO_DHase_a-bundle.
IPR010047; CO_DHase_cat.
IPR004137; Prismane.
IPR016099; Prismane-like_a/b-sand.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1270.30; CO_DH_a-bundle; 1.
G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 2.

Pfam

PF03063; Prismane; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005023; CODH; 1.

PRINTS

PR01415; ANKYRIN.

TIGRFAMs

TIGR01702; CO_DH_cata; 1.

Other

P27989; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; 4Fe-4S; Carbon dioxide fixation; Electron transport; Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 674`	`674`	`Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta.`	`PRO_0000079808`
`METAL`	`59 59`		`Iron-sulfur 1 (4Fe-4S); shared with dimeric partner.`
`METAL`	`67 67`		`Iron-sulfur 1 (4Fe-4S); shared with dimeric partner.`
`METAL`	`68 68`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`71 71`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`76 76`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`90 90`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`283 283`		`Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen.`
`METAL`	`317 317`		`Nickel-iron-sulfur (Ni-4Fe-4S).`
`METAL`	`355 355`		`Nickel-iron-sulfur (Ni-4Fe-4S).`
`METAL`	`470 470`		`Nickel-iron-sulfur (Ni-4Fe-4S).`
`METAL`	`500 500`		`Nickel-iron-sulfur (Ni-4Fe-4S).`
`METAL`	`550 550`		`Nickel-iron-sulfur (Ni-4Fe-4S).`
`STRAND`	`18 21`	`4`
`HELIX`	`31 42`	`12`
`HELIX`	`48 55`	`8`
`HELIX`	`60 63`	`4`
`STRAND`	`81 83`	`3`
`HELIX`	`94 128`	`35`
`HELIX`	`140 149`	`10`
`HELIX`	`159 175`	`17`
`HELIX`	`184 187`	`4`
`HELIX`	`192 200`	`9`
`HELIX`	`208 219`	`12`
`HELIX`	`227 256`	`30`
`STRAND`	`262 267`	`6`
`HELIX`	`268 270`	`3`
`STRAND`	`275 283`	`9`
`HELIX`	`285 296`	`12`
`HELIX`	`299 304`	`6`
`STRAND`	`310 315`	`6`
`HELIX`	`316 326`	`11`
`STRAND`	`330 332`	`3`
`HELIX`	`334 336`	`3`
`HELIX`	`337 341`	`5`
`STRAND`	`348 351`	`4`
`STRAND`	`353 355`	`3`
`HELIX`	`360 364`	`5`
`TURN`	`365 368`	`4`
`STRAND`	`370 373`	`4`
`STRAND`	`383 385`	`3`
`HELIX`	`390 392`	`3`
`HELIX`	`393 412`	`20`
`STRAND`	`425 429`	`5`
`HELIX`	`433 441`	`9`
`HELIX`	`448 457`	`10`
`STRAND`	`463 467`	`5`
`HELIX`	`479 490`	`12`
`STRAND`	`493 498`	`6`
`HELIX`	`499 507`	`9`
`TURN`	`508 511`	`4`
`HELIX`	`513 515`	`3`
`HELIX`	`516 519`	`4`
`HELIX`	`522 534`	`13`
`STRAND`	`543 550`	`8`
`HELIX`	`553 567`	`15`
`HELIX`	`571 573`	`3`
`STRAND`	`574 580`	`7`
`HELIX`	`586 597`	`12`
`STRAND`	`601 606`	`6`
`TURN`	`609 612`	`4`
`HELIX`	`614 621`	`8`
`HELIX`	`623 627`	`5`
`STRAND`	`631 634`	`4`
`HELIX`	`638 665`	`28`

Sequence information

Length: 674 AA [This is the length of the unprocessed precursor]

Molecular weight: 72924 Da [This is the MW of the unprocessed precursor]

CRC64: 54BA3D816C25F9FC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPRFRDLSHN CRPSEAPRVM EPKNRDRTVD PAVLEMLVKS KDDKVITAFD RFVAQQPQCK 

        70         80         90        100        110        120 
IGYEGICCRF CMAGPCRIKA TDGPGSRGIC GASAWTIVAR NVGLMILTGA AAHCEHGNHI 

       130        140        150        160        170        180 
AHALVEMAEG KAPDYSVKDE AKLKEVCRRV GIEVEGKSVL ELAQEVGEKA LEDFRRLKGE 

       190        200        210        220        230        240 
GEATWLMTTI NEGRKEKFRT HNVVPFGIHA SISELVNQAH MGMDNDPVNL VFSAIRVALA 

       250        260        270        280        290        300 
DYTGEHIATD FSDILFGTPQ PVVSEANMGV LDPDQVNFVL HGHNPLLSEI IVQAAREMEG 

       310        320        330        340        350        360 
EAKAAGAKGI NLVGICCTGN EVLMRQGIPL VTSFASQELA ICTGAIDAMC VDVQCIMPSI 

       370        380        390        400        410        420 
SAVAECYHTR IITTADNAKI PGAYHIDYQT ATAIESAKTA IRMAIEAFKE RKESNRPVYI 

       430        440        450        460        470        480 
PQIKNRVVAG WSLEALTKLL ATQNAQNPIR VLNQAILDGE LAGVALICGC NNLKGFQDNS 

       490        500        510        520        530        540 
HLTVMKELLK NNVFVVATGC SAQAAGKLGL LDPANVETYC GDGLKGFLKR LGEGANIEIG 

       550        560        570        580        590        600 
LPPVFHMGSC VDNSRAVDLL MAMANDLGVD TPKVPFVASA PEAMSGKAAA IGTWWVSLGV 

       610        620        630        640        650        660 
PTHVGTMPPV EGSDLIYSIL TQIASDVYGG YFIFEMDPQV AARKILDALE YRTWKLGVHK 

       670 
EVAERYETKL CQGY

P27989 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools