ID   COOS_ARCFU              Reviewed;         622 AA.
AC   O28429;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Carbon monoxide dehydrogenase;
DE            Short=CODH;
DE            EC=1.2.99.2;
GN   Name=cooS; OrderedLocusNames=AF_1849;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- CATALYTIC ACTIVITY: CO + H(2)O + A = CO(2) + AH(2).
CC   -!- COFACTOR: Binds 3 4Fe-4S clusters per homodimer (By similarity).
CC   -!- COFACTOR: Binds 2 nickel-iron-sulfur clusters per homodimer (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe4S cluster;
CC       cluster C is a mixed Ni-Fe-S cluster which appears to be the
CC       active site of CO oxidation. Cluster D is also an all-cysteinyl-
CC       liganded 4Fe4S cluster that bridges the two subunits of the CODH
CC       dimer (By similarity).
CC   -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide
CC       dehydrogenase family.
CC   -!- CAUTION: This protein lacks the conserved Cys in positions 48 and
CC       292; they are replaced by a Ser and a Glu, respectively. It is
CC       therefore possible that the C- and D-clusters are either altered
CC       or missing in this protein, which may not form homodimers.
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DR   EMBL; AE000782; AAB89403.1; -; Genomic_DNA.
DR   PIR; H69480; H69480.
DR   RefSeq; NP_070675.1; -.
DR   HSSP; Q9F8A8; 1JJY.
DR   GeneID; 1485070; -.
DR   GenomeReviews; AE000782_GR; AF_1849.
DR   KEGG; afu:AF1849; -.
DR   NMPDR; fig|224325.1.peg.1836; -.
DR   TIGR; AF_1849; -.
DR   HOGENOM; O28429; -.
DR   OMA; O28429; YMEQKAT.
DR   BioCyc; AFUL224325:AF_1849-MON; -.
DR   BRENDA; 1.2.99.2; 7576.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) ac...; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016101; CO_DH_a-bundle.
DR   InterPro; IPR010047; CO_DH_cat.
DR   InterPro; IPR004137; Prismane.
DR   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   Gene3D; G3DSA:1.20.1270.30; CO_DH_a-bundle; 1.
DR   Gene3D; G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 1.
DR   Pfam; PF03063; Prismane; 1.
DR   PIRSF; PIRSF005023; CODH; 1.
DR   TIGRFAMs; TIGR01702; CO_DH_cata; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel;
KW   Oxidoreductase.
FT   CHAIN         1    622       Carbon monoxide dehydrogenase.
FT                                /FTId=PRO_0000157140.
FT   METAL        40     40       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner (By similarity).
FT   METAL        49     49       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL        52     52       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL        57     57       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL        68     68       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       256    256       Nickel-iron-sulfur (By similarity).
FT   METAL       334    334       Nickel-iron-sulfur (By similarity).
FT   METAL       442    442       Nickel-iron-sulfur (By similarity).
FT   METAL       473    473       Nickel-iron-sulfur (By similarity).
FT   METAL       514    514       Nickel-iron-sulfur (By similarity).
SQ   SEQUENCE   622 AA;  67496 MW;  018304F4C49177B4 CRC64;
     MKIEGKVSEH ESINMMYERV SKEGVTNIVD RFNAQEKGRC PFCEKGLSCQ LCSMGPCRIS
     KDKPTGACGI DAAGMVVRNF THKNMLGTEA YTYHAIEAAK TLKATAEGKT IYEIKDVEKL
     KWFAKLLGIE GEDVNELAAK VADFVISDLS SLEKSRLVEI FAPEKRKELW EKLGIFPSGV
     FQELLTMGSS AMTNVDSNYV SLAKKSMSMS IATCMAAQIA LETIQDILFG TPMPHESHSD
     LGILDPEYVN IAVNGHEPFV GIALIKLAER EEIQEKARKA GAKGLRIIGF IETGQEILQR
     VDSPVFAGIV GNWIVQEYAL ATGCVDVFAA DMNCTLPSLP EYQRYGVKIV PVSRLVRLKG
     IDEGLDYEPE KAEEIAMKLI DMAIENFKQR DKSKAVKVEQ KKKIVVGFSP EAILKALNGD
     LNVLLDAIKK GDIKGVVALV SCTTLKNGPH DSSTVTIAKE LIKRDILVLS MGCGNAALQV
     AGLTSMEAVE LAGEKLKAVC KALNIPPVLS FGTCTDTGRA AYLVRLIADA LGVDVPQLPV
     AVTAPEYMEQ KATIDAVFAV AYGLTTHVSP VPPITGSEDA VKLFTEDVEK LTGGKVVVEE
     DPLKAAELLE KVIEEKRKAL GI
//