Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O27743 (ACDA_METTH)

Last modified February 9, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetyl-CoA decarbonylase/synthase complex subunit alpha
      Short name=ACDS complex subunit alpha
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase
      Short name=ACDS CODH
Gene names
Name: cdhA
Ordered Locus Names: MTH_1708
OrganismMethanobacterium thermoautotrophicum [Complete proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO2 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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 780780Acetyl-CoA decarbonylase/synthase complex subunit alpha HAMAP MF_01137
PRO_0000155085

Regions

Domain399 – 429314Fe-4S ferredoxin-type 1
Domain440 – 469304Fe-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 binding931Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2501Nickel-iron-sulfur By similarity
Metal binding2781Nickel-iron-sulfur By similarity
Metal binding3171Nickel-iron-sulfur By similarity
Metal binding4091Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4121Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4151Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4191Iron-sulfur 3 (4Fe-4S) Potential
Metal binding4491Iron-sulfur 4 (4Fe-4S) Potential
Metal binding4521Iron-sulfur 4 (4Fe-4S) Potential
Metal binding4551Iron-sulfur 4 (4Fe-4S) Potential
Metal binding4591Iron-sulfur 4 (4Fe-4S) Potential
Metal binding5171Nickel-iron-sulfur By similarity
Metal binding5461Nickel-iron-sulfur By similarity
Metal binding5811Nickel-iron-sulfur By similarity

Sequences

Sequence LengthMass (Da)Tools
O27743-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 98AB06D10C300685

FASTA78086,068
        10         20         30         40         50         60 
MIDVAPESKK AKDLKGDFWD AKNIQISIGE IITEEKPPEE EVKGPKPRPH VTDLRSWDMK 

        70         80         90        100        110        120 
LLERYEPFYA PFCDMCCLCT YGKCELLGKK GACGIDAATQ QARTVLLACL IGTAAHAGHA 

       130        140        150        160        170        180 
RHLVDHLIER LGEDYKIDLG SNVDIEAPIT RTVMGKRPAT LGDLREVMDY AEEQMSHLLS 

       190        200        210        220        230        240 
ACHTGQEGDS KDFESKAFHA GLMDDLTREV ADLAQIVALD LPKGDEDAPL VELGFGTIDT 

       250        260        270        280        290        300 
EKPVVLCIGH NVLPGADIVD YLDENEMEDQ VEVCGICCAA IDVTRYNEAA KVVGPLSKQL 

       310        320        330        340        350        360 
RFIRSGVADV IVVDEQCVRT DVLEEALKNR SAVIATTDKM CLGLPDMTDE DPDKIVNDLI 

       370        380        390        400        410        420 
NGNIEGALIL DPEKVGEVAV KTAMKLAPIR KSLKKLPDID EIIELASECT DCGWCQRVCP 

       430        440        450        460        470        480 
NSLPVMDAVK KAADGDLSKL EEMAIEELCY TCGRCEQECE RNIPIVSMVT KAGERRVKDE 

       490        500        510        520        530        540 
KYRIRAGRGP AQDVEIRRVG APIVLGDIPG VVAFVGCSNY PEGGKDVALM AKEFLERNYI 

       550        560        570        580        590        600 
VVTTGCGAMS IGEYRDEDGQ TLYEKYGGQF DAKGLVNMGS CVSNAHVSGA AIKIANIFAQ 

       610        620        630        640        650        660 
KPLEGNFEEI ADYILNRVGA CGVAWGAYSQ KAAAIATGVN RWGIPVVLGP HGSKYRRLFL 

       670        680        690        700        710        720 
GRADDEEKWK LKDLRTGEVI DGEPAPEHLL YAAENREEAT VMIAKLCIRP TDTPKGRQMK 

       730        740        750        760        770        780 
LSNYIDLHRK YLGTIPDDID RFIRTEKDIP IVYKRDVMKI LEEKNWKPRE LPKEPSLLER 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB86180.1.
PIRE69095.
RefSeqNP_276820.1.

3D structure databases

SMRO27743. Positions 43-778.
ModBaseSearch...

Protein-protein interaction databases

STRINGO27743.

Genome annotation databases

GeneID1470793.
GenomeReviewsGene locus MTH_1708 in contig AE000666_GR.
KEGGmth:MTH1708.
NMPDRfig|187420.1.peg.1675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04918.
HOGENOMHBG539676.
OMAICCTAID.

Enzyme and pathway databases

BioCycMTHE187420:MTH1708-MONOMER.
BRENDA1.2.99.2. 270.

Family and domain databases

HAMAPMF_01137. CdhA.
[Tree]
InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR004460. CO_DH/Ac-CoA_synth_asu.
IPR016101. CO_DH_a-bundle.
IPR004137. Prismane.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
Gene3DG3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit.
G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 2 hits.
PfamPF03063. Prismane. 2 hits.
[Graphical view]
TIGRFAMsTIGR00314. cdhA. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACDA_METTH
AccessionPrimary (citable) accession number: O27743
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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