[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. STRAIN=DSM 1825 / TM-1; PubMed=8955306 [NCBI, ExPASy, EBI, Israel, Japan] Maupin-Furlow J.A., Ferry J.G.; "Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of Methanosarcina thermophila."; J. Bacteriol. 178:6849-6856(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107, AND PROTEIN SEQUENCE OF 2-20. STRAIN=DSM 1825 / TM-1; PubMed=7693685 [NCBI, ExPASy, EBI, Israel, Japan] Sowers K.R., Thai T.T., Gunsalus R.P.; "Transcriptional regulation of the carbon monoxide dehydrogenase gene (cdhA) in Methanosarcina thermophila."; J. Biol. Chem. 268:23172-23178(1993).
[3]	CHARACTERIZATION. PubMed=11607176 [NCBI, ExPASy, EBI, Israel, Japan] Abbanat D.R., Ferry J.G.; "Resolution of component proteins in an enzyme complex from Methanosarcina thermophila catalyzing the synthesis or cleavage of acetyl-CoA."; Proc. Natl. Acad. Sci. U.S.A. 88:3272-3276(1991).

Comments

FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy (By similarity).
CATALYTIC ACTIVITY: CO + H₂O + A = CO₂ + AH₂.
COFACTOR: Binds 7 4Fe-4S clusters per heterotetramer (Potential).
COFACTOR: Binds 2 nickel-iron-sulfur clusters per heterotetramer (Potential).
PATHWAY: One-carbon metabolism; methanogenesis from acetate .
SUBUNIT: Heterotetramer of two alpha and two epsilon chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).
DOMAIN: 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. May contain two additional 4Fe-4S clusters, dubbed E and F, that might reroute electron transfer along different paths.
SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family.
SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.

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

U66032; AAC44650.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L20952; AAA72034.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48868; A48868.

3D structure databases

ModBase

Q08368.

Ontologies

GO:0018492;	Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01137; -; 1.
PBIL [Tree]

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR004460; CO_DHase/Ac-CoA_synth_asu.
IPR016101; CO_DHase_a-bundle.
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

PF00037; Fer4; 2.
PF03063; Prismane; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00314; cdhA; 1.

PROSITE

PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel; Oxidoreductase; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 806`	`805`	`Acetyl-CoA decarbonylase/synthase complex subunit alpha 1.`	`PRO_0000155083`
`DOMAIN`	`407 436`	`30`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`445 475`	`31`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`73 73`		`Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity).`
`METAL`	`76 76`		`Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity).`
`METAL`	`77 77`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`79 79`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`84 84`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`94 94`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`250 250`		`Nickel-iron-sulfur (By similarity).`
`METAL`	`278 278`		`Nickel-iron-sulfur (By similarity).`
`METAL`	`323 323`		`Nickel-iron-sulfur (By similarity).`
`METAL`	`417 417`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`420 420`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`423 423`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`427 427`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`455 455`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`458 458`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`461 461`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`465 465`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`523 523`		`Nickel-iron-sulfur (By similarity).`
`METAL`	`552 552`		`Nickel-iron-sulfur (By similarity).`
`METAL`	`587 587`		`Nickel-iron-sulfur (By similarity).`

Sequence information

Length: 806 AA [This is the length of the unprocessed precursor]

Molecular weight: 88538 Da [This is the MW of the unprocessed precursor]

CRC64: 6CC1BB8A6DFEBD61 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKLTTGSFS IEDLESVQIT INNVIGAAKE AADEKAKDLG PMGPSAWPGL ATYRDDWNLK 

        70         80         90        100        110        120 
LLDRYEPVIT PMCDQCCYCT YGPCDLSNNK RGACGIDMLG HNGREFFLRV ITGTACHAAH 

       130        140        150        160        170        180 
GRHLLDHLIE VFGEDLPLKL GQSDVLTPNI TITTGQRPMT LGEIKPAMEH TEEQLTQLLA 

       190        200        210        220        230        240 
TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDIVQIAALD FPKADPEAPL IEMGVGTIDK 

       250        260        270        280        290        300 
EKPFLCVIGH NVGGVTYMMD YMEEHDLTGK MELGGLCCTA IDLTRYKEAD RRAPYTKVIG 

       310        320        330        340        350        360 
SMSQELKIIR SGLPDVIVVD EQCVRGDIVP EAQKLGIPVI ASNAKIMYGL PNRDEQDVDA 

       370        380        390        400        410        420 
TIEELKSGAI PGAVILDYDK LGEISVRLTQ EMHPLREAAG LRKIASDEQM KEWVDKCADC 

       430        440        450        460        470        480 
GSCYLVCPEE LEIPEAMKHA KEGDYSYLVD LHDQCIGCRR CEQVCKKEIP ILSVIEKASQ 

       490        500        510        520        530        540 
KVIAEEKGWM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYGDGA KSVYYIAEEF 

       550        560        570        580        590        600 
LKRNFIVVGT GCGAMDMGMY KDENGQTLYE RFPGGFQSGG LVNIGSCVSN AHITGAAQKV 

       610        620        630        640        650        660 
AGIFGGRTME GNLAEIADYV LNRVGACGLA WGAFSQKASS IGTGCNIYGI PAVLGPHSSK 

       670        680        690        700        710        720 
YRRALISKNY DDEKWKVYDA RSGEEMAIPP APEFLLITAE TWQEAIPMMA KACIRPSDNS 

       730        740        750        760        770        780 
MGRSIKLTHW MELHQKYIGG MPEDWWKFIR TEADLPLAKR AELMKKLEEE HGWEIDWKRK 

       790        800 
KIISGPKIKF DVSAQPTNLK RLCKGA

Q08368 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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