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UniProtKB/Swiss-Prot entry O30274

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

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Entry information
Entry name ACDA2_ARCFU
Primary accession number O30274
Secondary accession numbers None
Integrated into Swiss-Prot on November 21, 2003
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 56)
Name and origin of the protein
Protein name Acetyl-CoA decarbonylase/synthase complex subunit alpha 2
Synonyms ACDS complex subunit alpha 2
EC 1.2.99.2
ACDS complex carbon monoxide dehydrogenase 2
ACDS CODH 2
Gene name
Name: cdhA2
OrderedLocusNames: AF_2397
From
Archaeoglobus fulgidus [TaxID: 2234] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; Archaeoglobus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
DOI=10.1038/37052; PubMed=9389475 [NCBI, ExPASy, EBI, Israel, Japan]
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(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
AE000782; AAB91266.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F69549; F69549.
RefSeq NP_071219.1; -.
3D structure databases
HSSP P00198; 1FCA. [HSSP ENTRY / PDB]
ModBase O30274.
Enzyme and pathway databases
BioCyc AFUL224325:AF_2397-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.
PRINTS PR00353; 4FE4SFRDOXIN.
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 1485627; -.
GenomeReviews AE000782_GR; AF_2397.
KEGG afu:AF2397; -.
NMPDR fig|224325.1.peg.2381; -.
TIGR AF_2397; -.
Phylogenomic databases
HOGENOM O30274; -.
Other
ProtoNet O30274.
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   798  798     Acetyl-CoA decarbonylase/synthase complex subunit alpha 2. PRO_0000155073
DOMAIN   395   424  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   434   463  30     4Fe-4S ferredoxin-type 2. 
METAL   65    65        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   68    68        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   69    69        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   71    71        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   76    76        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   86    86        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   246   246        Nickel-iron-sulfur (By similarity). 
METAL   274   274        Nickel-iron-sulfur (By similarity). 
METAL   313   313        Nickel-iron-sulfur (By similarity). 
METAL   405   405        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   408   408        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   411   411        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   415   415        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   443   443        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   446   446        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   449   449        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   453   453        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   511   511        Nickel-iron-sulfur (By similarity). 
METAL   540   540        Nickel-iron-sulfur (By similarity). 
METAL   575   575        Nickel-iron-sulfur (By similarity). 
Sequence information
Length: 798 AA [This is the length of the unprocessed precursor] Molecular weight: 88378 Da [This is the MW of the unprocessed precursor] CRC64: FC3CBCCB41BD30A0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVLEFGKGAF VVDDLRNVTI KIGEIAEEEE EWAPMGPTPM PGIATLRDWD FFLLKRYKPF 

        70         80         90        100        110        120 
YAPACDMCCL CTMGKCDLTG NKRGACGIDL AAQTGRIVTI ACSIGVSAHT GHARHMLHDI 

       130        140        150        160        170        180 
EHMTGKKLSE IPVDLGPEID EVAPLTELIT GIKPKTLEDL ERALRYAEEQ IVQVVDAVHT 

       190        200        210        220        230        240 
GQEGSYLDYE SKALHLGMLD SLGKEIADIA QICAFGYPKG EDNQPLIEVG MGVMDRSKAM 

       250        260        270        280        290        300 
ILVIGHHAPP VLNIADYIEE NGLEDEVDLG GICCTANDMT RYYQKAKIVS ALGRQLKVIR 

       310        320        330        340        350        360 
AGLADVIVID EQCIRADILY HTKKLGIPVI CTNEKAMHAL PDMTKEEPKN IIKYLLDGNP 

       370        380        390        400        410        420 
GCVILDPLKV GEVAVEVARA RRKQRGDDIG PRLTEEQFME YARACTQCGN CTIACPQGIR 

       430        440        450        460        470        480 
IGEAMEAAEN GDRSKLEKEW DVCIACGRCE QVCPKGIPII DMYNYAAWNL IVNEKGKLRR 

       490        500        510        520        530        540 
GRGPIRDSEI RNVGAPIVLG TIPGIIAVIG CGNYPNGTRD AYTIMDEFAS RNYIVVTTGC 

       550        560        570        580        590        600 
MAFDAALYKD EEGQTVYEKY HDRFDGGGVV QIGSCVANAH IHGAAIKVAR IFAKRNIRAN 

       610        620        630        640        650        660 
YEEIADYILN RVGACGVAWG AYSQKAASIA TGFNRLGIPA VVGPHGSKYR RAFLGRPYND 

       670        680        690        700        710        720 
EDWMVYDART GEKVRIEPAP QDLLVAAETI EEAIPLMAKL CFRPNDTTQG RSIKLTHYID 

       730        740        750        760        770        780 
LSLKYLKRMP DDWHLFVRTE ADLPLAKKEE LLKELEDKHG WKIDWQKKKI VEGPIRGYHA 

       790 
GFNPTNLERC LRDGFMTV
O30274 in FASTA format

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