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Q49161 (ACDA1_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina ›

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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-Rule MF_01137

Catalytic activity

CO + H2O + A = CO2 + AH2. HAMAP-Rule 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-Rule 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-Rule 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-Rule MF_01137

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 806805Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 HAMAP-Rule MF_01137
PRO_0000155080

Regions

Domain406 – 436314Fe-4S ferredoxin-type 1
Domain445 – 475314Fe-4S ferredoxin-type 2

Sites

Metal binding731Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity
Metal binding771Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding791Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding841Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding941Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2501Nickel-iron-sulfur By similarity
Metal binding2781Nickel-iron-sulfur By similarity
Metal binding3231Nickel-iron-sulfur By similarity
Metal binding4171Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4201Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4231Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4271Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4551Iron-sulfur 4 (4Fe-4S) Potential
Metal binding4581Iron-sulfur 4 (4Fe-4S) Potential
Metal binding4611Iron-sulfur 4 (4Fe-4S) Potential
Metal binding4651Iron-sulfur 4 (4Fe-4S) Potential
Metal binding5231Nickel-iron-sulfur By similarity
Metal binding5521Nickel-iron-sulfur By similarity
Metal binding5871Nickel-iron-sulfur By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49161 [UniParc].

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

FASTA80688,583
        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

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12.
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / 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. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L26487 Genomic DNA. Translation: AAC37044.1.
AE008384 Genomic DNA. Translation: AAM31785.1.
RefSeqNP_634113.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ49161.
SMRQ49161. Positions 43-804.
ModBaseSearch...

Protein-protein interaction databases

STRING192952.MM_2089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM31785; AAM31785; MM_2089.
GeneID1480431.
KEGGmma:MM_2089.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1152.
HOGENOMHOG000224351.
KOK00192.
OMAVANSHIA.
ProtClustDBPRK00941.

Enzyme and pathway databases

UniPathwayUPA00642.

Family and domain databases

Gene3D3.40.50.2030. 2 hits.
HAMAPMF_01137. CdhA.
InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR004460. CO_DH/Ac-CoA_synth_asu.
IPR004137. HCP/CODH.
IPR009051. Helical_ferredxn.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamPF13183. Fer4_8. 1 hit.
PF03063. Prismane. 2 hits.
[Graphical view]
SUPFAMSSF46548. Helical_ferredxn. 1 hit.
SSF56821. Prismane_like. 1 hit.
TIGRFAMsTIGR00314. cdhA. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACDA1_METMA
AccessionPrimary (citable) accession number: Q49161
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents