Acetyl-CoA decarbonylase/synthase complex subunit alpha 2

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Reviewed, UniProtKB/Swiss-Prot Q49163 (ACDA2_METMA)

Last modified February 9, 2010. Version 76. 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 2
      Short name=ACDS complex subunit alpha 2
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase 2
      Short name=ACDS CODH 2

Gene names

Name:	cdhA2
Ordered Locus Names:	MM_0684

Organism

Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]

Taxonomic identifier

2209 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

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Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 Direct protein sequencing
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

Initiator methionine

Removed Ref.1

Chain

2 – 807

806

Acetyl-CoA decarbonylase/synthase complex subunit alpha 2 HAMAP MF_01137

PRO_0000155081

Regions

Domain

407 – 436

4Fe-4S ferredoxin-type 1

Domain

446 – 475

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

250

Nickel-iron-sulfur By similarity

Metal binding

278

Nickel-iron-sulfur By similarity

Metal binding

323

Nickel-iron-sulfur By similarity

Metal binding

417

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

Metal binding

420

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

Metal binding

423

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

Metal binding

427

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

Metal binding

455

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

Metal binding

458

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

Metal binding

461

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

Metal binding

465

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

Metal binding

523

Nickel-iron-sulfur By similarity

Metal binding

552

Nickel-iron-sulfur By similarity

Metal binding

587

Nickel-iron-sulfur By similarity

Experimental info

Sequence conflict

W → R in AAC37042. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q49163-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E00F628DC63C52BD
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FASTA

807

88,508

        10         20         30         40         50         60 
MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELV KAGPTLFPGL ESYRDDWNFK 

        70         80         90        100        110        120 
LLDRYEPVVT PMCDQCCYCT YGPCDLSGNK RGACGIDMMG HNGREFFLRV ITGTACHAAH 

       130        140        150        160        170        180 
GRHLLDHLIE TFGEDLPLNL GQSNVLTPNI TISTGLSPKN LGEVKPAMEF VEEQLTQLLA 

       190        200        210        220        230        240 
TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDVVQVAAYD FPKADPEAPL IEIGMGTIDK 

       250        260        270        280        290        300 
SKPFLCVIGH NVGGVTYMMD YMEENNLTDK MEIAGLCCTA IDLTRYKEAD RRPPYAKVIG 

       310        320        330        340        350        360 
SMAKELKVIR SGMPDVIVVD EQCVRGDIVP EAQKLKIPVI ASNAKIMFGL PNRTDADVNE 

       370        380        390        400        410        420 
TIEELKSGAI PGCVMLDYEK LGELCIRLTM EMAPIRDASG ITAIPTDEEL ANWVAKCADC 

       430        440        450        460        470        480 
GACLIACPEE LDIPEAMGFA KEGDYSYLEG LHDICIGCRR CEQVCKKEIP ILNIIEKVSQ 

       490        500        510        520        530        540 
KQIAEEKGWM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYAEGT KDVYYIAEEF 

       550        560        570        580        590        600 
LKRNFIVVTT GCGAMDIGMF KDDDGKTLYE RYPGGFQCGG LVNIGSCVSN AHITGAAEKV 

       610        620        630        640        650        660 
AAIFAQRTLE GNLAEIADYI LNRVGACGLA WGAFSQKASS IGTGCNILGI PAVLGPHSSK 

       670        680        690        700        710        720 
YRRALIAKTY EEDKWKVYDA RNGQEMPIPP APEFLLTTAE TWQEAIPMMA KACIRPSDNS 

       730        740        750        760        770        780 
MGRAIKLTHW MELHKKYLGG SEPEDWWKFV RNEADLPLAN REALLKKLEA ERGWEIDWKK 

       790        800 
KKIISGPKIK FDVSAQPTNL KRLCKEA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters." Eggen R.I.L., van Kranenburg R., Vriesema A.J.M., Geerling A.C.M., Verhagen M.F.J.M., Hagen W.R., de Vos W.M. J. Biol. Chem. 271:14256-14263(1996) [PubMed: 8662887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12 AND 560-564. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.
[2]	"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. Gottschalk G. J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	L26486 Genomic DNA. Translation: AAC37042.1. AE008384 Genomic DNA. Translation: AAM30380.1.
RefSeq	NP_632708.1.
3D structure databases
SMR	Q49163. Positions 42-806.
ModBase	Search...
Genome annotation databases
GeneID	1479026.
GenomeReviews	Gene locus MM_0684 in contig AE008384_GR.
KEGG	mma:MM_0684.
NMPDR	fig\|192952.1.peg.684.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG539676.
OMA	ICCTAID.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM0684-MONOMER.
BRENDA	1.2.99.2. 261165.
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

ACDA2_METMA

Accession

Primary (citable) accession number: Q49163

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 76 of the entry and version 4 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

Experimental info

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