Acetyl-CoA decarbonylase/synthase complex subunit alpha 3

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Reviewed, UniProtKB/Swiss-Prot Q8THW2 (ACDA3_METAC)

Last modified January 19, 2010. Version 53. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Acetyl-CoA decarbonylase/synthase complex subunit alpha 3
      Short name=ACDS complex subunit alpha 3
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase 3
      Short name=ACDS CODH 3

Gene names

Name:	cdhA3
Ordered Locus Names:	MA_4399

Organism

Methanosarcina acetivorans [Complete proteome] [HAMAP]

Taxonomic identifier

2214 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

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Protein attributes

Sequence length	805 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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General annotation (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. HAMAP MF_01137
Catalytic activity	CO + H₂O + A = CO₂ + AH₂. HAMAP MF_01137
Cofactor	Binds 7 4Fe-4S clusters per heterotetramer Potential. HAMAP MF_01137 Binds 2 nickel-iron-sulfur clusters per heterotetramer Potential. HAMAP MF_01137
Pathway	One-carbon metabolism; methanogenesis from acetate. HAMAP MF_01137
Subunit structure	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 (alpha₂epsilon₂)(4)-beta(8)-(gamma₁delta₁)₈ Potential. HAMAP MF_01137
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. HAMAP MF_01137
Sequence similarities	Belongs to the Ni-containing carbon monoxide dehydrogenase family. Contains 2 4Fe-4S ferredoxin-type domains.

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Ontologies

Keywords
Biological process	Methanogenesis
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: HAMAP electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 805

805

Acetyl-CoA decarbonylase/synthase complex subunit alpha 3 HAMAP MF_01137

PRO_0000155076

Regions

Domain

407 – 435

4Fe-4S ferredoxin-type 1

Domain

445 – 474

4Fe-4S ferredoxin-type 2

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

249

Nickel-iron-sulfur By similarity

Metal binding

277

Nickel-iron-sulfur By similarity

Metal binding

322

Nickel-iron-sulfur By similarity

Metal binding

416

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

419

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

422

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

426

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

454

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

457

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

460

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

464

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

522

Nickel-iron-sulfur By similarity

Metal binding

551

Nickel-iron-sulfur By similarity

Metal binding

586

Nickel-iron-sulfur By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8THW2-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 8B1B9B32B56C56CD
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FASTA

805

87,993

        10         20         30         40         50         60 
MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELG PMGPTAMAGL ASYRSWNLLL 

        70         80         90        100        110        120 
LDRYEPVLTP MCDQCCYCTY GPCDLSGNKR GACGIDMAGQ TGREFFLRVI TGTACHAAHG 

       130        140        150        160        170        180 
RHLLDHVIEV FGEDLPLNLG ESNVLTPNVT ICTGLSPKTL GECRAPMEYV EEQLTQLLAT 

       190        200        210        220        230        240 
IHAGQESAEI DYDSKALFSG SLDHVGMEVS DIAQVSAYDF PKADPEAPLI EIGMGSIDKS 

       250        260        270        280        290        300 
KPLIVAIGHN VAGVTYIMDY MEENNLTDKM EIAGLCCTAF DMTRYKEADR RAPYAKIVGS 

       310        320        330        340        350        360 
LAKELKVIRS GMPDVIVVDE QCVRGDVLSE SMKLKIPVIA SNEKIMMGLP DRTDADVDSI 

       370        380        390        400        410        420 
VEEIKSGAIP GCVMLDYDKL GELIPKIAEV MAPIRDAEGI TAIPTDEEFK VYIDKCVKCG 

       430        440        450        460        470        480 
ECMLACPEEL DIPEALEYAA KGSYEYLEAL HDVCIGCRRC EQVCKKEIPI LNVLEKAAQK 

       490        500        510        520        530        540 
SISEEKGWVR SGRGQASDAE IRAEGLNLVM GTTPGIIAII GCPNYPAGTK DVYNIAEEFL 

       550        560        570        580        590        600 
KRNYLVVVSG CSAMDIGMYK DDDGKTLYER YPGTFSGGGL LNTGSCVSNA HITGAAEKVA 

       610        620        630        640        650        660 
GIFAQRTLAG NLAEVADYTL NRVGACGLAW GAYSQKAASI GTGCNIYGIP AVLGPHSSKY 

       670        680        690        700        710        720 
RRALIAKTYE EDKWKVFDAR DGSEMNIPPA PEFLLTTAET WQEALPMMAK ACIRPSDNNM 

       730        740        750        760        770        780 
GRSIKLTHWM ELSKKYLGVE PEDWWKFVRN EADLPLAKRE ELLKRLEAEQ GWEIDWKRKK 

       790        800 
IISGPKIKFD VSAQPTNLKR LCKEA

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References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.

Birren B.
Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010299 Genomic DNA. Translation: AAM07741.1.
RefSeq	NP_619261.1.
3D structure databases
SMR	Q8THW2. Positions 43-804.
ModBase	Search...
Genome annotation databases
GeneID	1476293.
GenomeReviews	Gene locus MA_4399 in contig AE010299_GR.
KEGG	mac:MA4399.
NMPDR	fig\|188937.1.peg.4287.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG539676.
Enzyme and pathway databases
BioCyc	MACE188937:MA4399-MONOMER.
BRENDA	1.2.99.2. 275708.
Family and domain databases
HAMAP	MF_01137. CdhA. [Tree]
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR004460. CO_DH/Ac-CoA_synth_asu. IPR016101. CO_DH_a-bundle. IPR009051. Helical_ferredxn. 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.
Pfam	PF03063. Prismane. 2 hits. [Graphical view]
TIGRFAMs	TIGR00314. cdhA. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ACDA3_METAC

Accession

Primary (citable) accession number: Q8THW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	June 1, 2002
Last modified:	January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents