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UniProtKB/Swiss-Prot entry O27743

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACDA_METTH
Primary accession number O27743
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Acetyl-CoA decarbonylase/synthase complex subunit alpha
Synonyms ACDS complex subunit alpha
EC 1.2.99.2
ACDS complex carbon monoxide dehydrogenase
ACDS CODH
Gene name
Name: cdhA
OrderedLocusNames: MTH_1708
From
Methanobacterium thermoautotrophicum [TaxID: 187420] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Delta H;
PubMed=9371463 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.";
J. Bacteriol. 179:7135-7155(1997).
Comments
  • FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2) (By similarity).
  • CATALYTIC ACTIVITY: CO + H2O + A = CO2 + AH2.
  • COFACTOR: Binds 7 4Fe-4S clusters per heterotetramer (Potential).
  • COFACTOR: Binds 2 nickel-iron-sulfur clusters per heterotetramer (Potential).
  • SUBUNIT: 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 (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(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.
  • SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family.
  • SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE000666; AAB86180.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E69095; E69095.
RefSeq NP_276820.1; -.
3D structure databases
ModBase O27743.
Enzyme and pathway databases
BioCyc MTHE187420:MTH1708-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0018492; Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from HAMAP).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0006084; Biological process: acetyl-CoA metabolic process (inferred from electronic annotation from InterPro).
GO:0006091; Biological process: generation of precursor metabolites and energy (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01137; -; 1.
PBIL [Tree]
InterPro IPR001450; 4Fe4S_Fe_S_bd.
IPR004460; CO_DHase/Ac-CoA_synth_asu.
IPR016101; CO_DHase_a-bundle.
IPR004137; Prismane.
IPR016099; Prismane-like_a/b-sand.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1270.30; CO_DH_a-bundle; 1.
G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 2.
Pfam PF00037; Fer4; 2.
PF03063; Prismane; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00314; cdhA; 1.
PROSITE PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1470793; -.
GenomeReviews AE000666_GR; MTH_1708.
KEGG mth:MTH1708; -.
NMPDR fig|187420.1.peg.1675; -.
Phylogenomic databases
HOGENOM O27743; -.
Genome annotation databases
CMR O27743; MTH_1708.
Other
ProtoNet O27743.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   780  780     Acetyl-CoA decarbonylase/synthase complex subunit alpha. PRO_0000155085
DOMAIN   399   429  31     4Fe-4S ferredoxin-type 1. 
DOMAIN   440   469  30     4Fe-4S ferredoxin-type 2. 
METAL   73    73        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   76    76        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   77    77        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   79    79        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   84    84        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   93    93        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   250   250        Nickel-iron-sulfur (By similarity). 
METAL   278   278        Nickel-iron-sulfur (By similarity). 
METAL   317   317        Nickel-iron-sulfur (By similarity). 
METAL   409   409        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   412   412        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   415   415        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   419   419        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   449   449        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   452   452        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   455   455        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   459   459        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   517   517        Nickel-iron-sulfur (By similarity). 
METAL   546   546        Nickel-iron-sulfur (By similarity). 
METAL   581   581        Nickel-iron-sulfur (By similarity). 
Sequence information
Length: 780 AA [This is the length of the unprocessed precursor] Molecular weight: 86068 Da [This is the MW of the unprocessed precursor] CRC64: 98AB06D10C300685 [This is a checksum on the sequence] 
        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
O27743 in FASTA format

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