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UniProtKB/Swiss-Prot entry Q57617


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

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Entry information
Entry name ACDA_METJA
Primary accession number Q57617
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 15, 1998 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 55)
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: MJ0153
From
Methanocaldococcus jannaschii (Methanococcus jannaschii) [TaxID: 2190] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087 [NCBI, ExPASy, EBI, Israel, Japan]
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.";
Science 273:1058-1073(1996).
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
L77117; AAB98135.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64319; B64319.
RefSeq NP_247121.1; -.
3D structure databases
ModBase Q57617.
Enzyme and pathway databases
BioCyc MJAN243232:MJ_0153-MON; -.
Ontologies
GO
GO:0018492; Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from HAMAP).
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).
BLOCKS Q57617.
Genome annotation databases
GeneID 1450997; -.
GenomeReviews L77117_GR; MJ0153.
KEGG mja:MJ0153; -.
NMPDR fig|243232.1.peg.158; -.
TIGR MJ0153; -.
Phylogenomic databases
HOGENOM Q57617; -.
Other
ProtoNet Q57617.
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   774  774     Acetyl-CoA decarbonylase/synthase complex subunit alpha. PRO_0000155077
DOMAIN   398   427  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   436   466  31     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   94    94        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   251   251        Nickel-iron-sulfur (By similarity). 
METAL   279   279        Nickel-iron-sulfur (By similarity). 
METAL   318   318        Nickel-iron-sulfur (By similarity). 
METAL   408   408        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   411   411        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   414   414        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   418   418        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   446   446        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   449   449        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   452   452        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   456   456        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   514   514        Nickel-iron-sulfur (By similarity). 
METAL   543   543        Nickel-iron-sulfur (By similarity). 
METAL   578   578        Nickel-iron-sulfur (By similarity). 
Sequence information
Length: 774 AA [This is the length of the unprocessed precursor] Molecular weight: 85900 Da [This is the MW of the unprocessed precursor] CRC64: F7CFD66F15CB1C7E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVMGNNVEMD IKKLLTPLVK MKNANISMSI KFGEEEEEEW EPMGPTPMPK IPTLRHWDFK 

        70         80         90        100        110        120 
LLERYPPFYM PICDLCCLCT FGKCDLSRGK KGACGLNIKA QQARIVLIAC CIGAACHAGH 

       130        140        150        160        170        180 
SRHLVHHLIE TLGRDYPIDL GNEIEVEAPI ARTVTGIKPK TLGDLEKILD YCEEQITHLL 

       190        200        210        220        230        240 
SAAHTGQEGD YLDFESKALH AGMIDDLARE AGDLAQIVAY NMPKGDEDAP LIELGFGCID 

       250        260        270        280        290        300 
KSKPVILCIG HNVVPGSYIL EYLEENSMED EVEVCGICCT AIDITRVSDK PKVVGPLSRQ 

       310        320        330        340        350        360 
LMFVRSGVAD VVIVDEQCIR TDILEEVLKT GAVLIATNEK MCLGLEDVSH MDEDEIIGYL 

       370        380        390        400        410        420 
LRNRAALLLD EKKVGKVAVE VAKIVAKERK DRKTLPDLNE VVELAKQCTE CGWCNRNCPN 

       430        440        450        460        470        480 
AFKVKEAMAL AKQGNFKGFI DLYKRCYGCG RCEAICPRNL PIVSMTTKVG EAYYKDLKFK 

       490        500        510        520        530        540 
MRAGRGPIKD VEIRSVGAPI VFGDIPGVVA LVGCSNHPNG EEEVAMIAKE FLERKYIVVA 

       550        560        570        580        590        600 
TGCAAMAIGM WKDKDGKTLY EKYPGEFRAG GLVNCGSCLS NCHITGAAIK IANIFAKVPL 

       610        620        630        640        650        660 
RGNYAEVADY ILNKVGAVGV AWGAMSQKAA AIATGVNRWG IPVILGPHGA KYRRLYLSNG 

       670        680        690        700        710        720 
EKFKVKDKKT GEILEIEPAP EHLIVTAENV KECICMIPKL CMRPNDTPKG RANKIYHYVD 

       730        740        750        760        770 
VYEKYFGRMP PDLEKFVRTE KDIPFMMKDK IMAYLEEKGW KPLEKYPQDP TILY 

Q57617 in FASTA format

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