Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

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Reviewed, UniProtKB/Swiss-Prot Q49161 (ACDA1_METMA)

Last modified June 16, 2009. Version 71. History...

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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 1
      Short name=ACDS complex subunit alpha 1
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase 1
      Short name=ACDS CODH 1

Gene names

Name:	cdhA1
Ordered Locus Names:	MM_2089

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	806 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.
Catalytic activity	CO + H₂O + A = CO₂ + AH₂. HAMAP MF_01137
Cofactor	Binds 7 4Fe-4S clusters per heterotetramer Potential. Binds 2 nickel-iron-sulfur clusters per heterotetramer Potential.
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.
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.
biophysicochemical properties	pH dependence: Optimum pH is 8-9. HAMAP MF_01137

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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 – 806

805

Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 HAMAP MF_01137

PRO_0000155080

Regions

Domain

406 – 436

4Fe-4S ferredoxin-type 1

Domain

445 – 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

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Sequences

Sequence

Length

Mass (Da)

Tools

Q49161-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8A6EE054FBE778AF
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FASTA

806

88,583

        10         20         30         40         50         60 
MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKTKELG HMGPTPFPGL ETYRDDWNLK 

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

       130        140        150        160        170        180 
GRHLLDHLIE VFGEELPLNL GQSDVLTPNI TITTGQRPQT LGEIKPAMEH VEEQLTQLLA 

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

       250        260        270        280        290        300 
DKPFLCVIGH NVGGVTYMMD YMEEHELTDK VELGGLCCTA IDLTRYKEAD RRPPYTKVVG 

       310        320        330        340        350        360 
SMSKELKIIR SGMPDVIVVD EQCVRGDIVP EAQKLKIPVI ASNAKIMYGL PNRTDAGVEE 

       370        380        390        400        410        420 
TIEELKSGAI PGAVILDYEK LGEISVRLAQ EMHPIREAAG VREIPSDEQL KEWVDKCADC 

       430        440        450        460        470        480 
GACYLACPIE LDIPEAMKFA KQGDFSYLED LHDACIGCRR CEQVCKKEIP ILSVIEKASQ 

       490        500        510        520        530        540 
KIIAEEKGWM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYSDCA KAVYYIAEEF 

       550        560        570        580        590        600 
LKRNYIVVGT GCGSMDMGMY KDEDGKTLYE RFPGGFQSGG LVNIGSCVSN AHITGAAQKV 

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

       670        680        690        700        710        720 
YRRALIAKNY DESKWKVYDA RNGEEMPIPP APEFLLTTAE TWQEAIPMMA KACLRPSDNS 

       730        740        750        760        770        780 
LGRSIKLTHW MELHDKYIGG LPEDWWKFIR TEADLPLAKR ADLMKKLEAE RGWEIDWKKK 

       790        800 
KIISGPKIKF DVSAQPTNLK RLCKGA

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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. 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
	L26487 Genomic DNA. Translation: AAC37044.1. AE008384 Genomic DNA. Translation: AAM31785.1.
RefSeq	NP_634113.1.
3D structure databases
HSSP	HSSP built from PDB template 1DUR based on UniProtKB P00193.
ModBase	Search...
Genome annotation databases
GeneID	1480431.
GenomeReviews	Gene locus MM_2089 in contig AE008384_GR.
KEGG	mma:MM_2089.
NMPDR	fig\|192952.1.peg.2089.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q49161.
OMA	Q49161. PNITITT.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM2089-MON.
BRENDA	1.2.99.2. 261165.
Family and domain databases
HAMAP	MF_01137. [Tree]
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR004460. CO_DH/Ac-CoA_synth_asu. IPR016101. CO_DH_a-bundle. IPR004137. Prismane. 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	PF00037. Fer4. 1 hit. PF03063. Prismane. 1 hit. [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

ACDA1_METMA

Accession

Primary (citable) accession number: Q49161

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 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