ID   COOS2_METMA             Reviewed;         634 AA.
AC   Q8PUN1;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Carbon monoxide dehydrogenase 2;
DE            Short=CODH 2;
DE            EC=1.2.99.2;
GN   Name=cooS2; OrderedLocusNames=MM_2301;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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 52 and
CC       300; they are replaced by an Arg and a Glu, respectively. It is
CC       therefore possible that the C- and D-clusters are either altered
CC       or missing in this protein.
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DR   EMBL; AE008384; AAM31997.1; -; Genomic_DNA.
DR   RefSeq; NP_634325.1; -.
DR   HSSP; Q9F8A8; 1JJY.
DR   GeneID; 1480643; -.
DR   GenomeReviews; AE008384_GR; MM_2301.
DR   KEGG; mma:MM_2301; -.
DR   NMPDR; fig|192952.1.peg.2301; -.
DR   HOGENOM; Q8PUN1; -.
DR   OMA; Q8PUN1; YMEQKAT.
DR   BioCyc; MMAZ192952:MM2301-MON; -.
DR   BRENDA; 1.2.99.2; 261165.
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; 2.
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    634       Carbon monoxide dehydrogenase 2.
FT                                /FTId=PRO_0000157146.
FT   METAL        44     44       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner (By similarity).
FT   METAL        53     53       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL        56     56       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL        61     61       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL        73     73       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       264    264       Nickel-iron-sulfur (By similarity).
FT   METAL       343    343       Nickel-iron-sulfur (By similarity).
FT   METAL       453    453       Nickel-iron-sulfur (By similarity).
FT   METAL       484    484       Nickel-iron-sulfur (By similarity).
FT   METAL       525    525       Nickel-iron-sulfur (By similarity).
SQ   SEQUENCE   634 AA;  69220 MW;  4C2B004AAB767190 CRC64;
     MDKERISYHE SVQKMYERIK ADNMTNVWDR YEAQGIGGVP DRRCTFCMAG ARCDLCSNGP
     CRSDASKDKR GVCGITADGM AMRMMLLRNV MGASTYHYHT DQTIRTLRET ARNKTPYSIR
     EPEKLKTFAN RLGIDISGSD AEIALNLCEF VEKDFNRPAY EPSRIVEILA PPERKKRWEE
     LGIFPGGIYG EMMLSTSSCL TNVDGYYVSL ALKAMRLGIA MAYQSQIVNE YCQDVLFGIP
     RPHTMRVDLG VLDPEYVNVL PNGHEPFLGF AMVQLARKPE WQEKAKAAGA KGLRVIASIE
     TGQEMIQRWE EDDVFYGFTG NWISQEAVLA SRCVDLFAAD MNCSLPVAPL YAEKYNFKLM
     PVSDLVAFEG IEERLNYDPV EAEEQAAKLL DMAVENFKNR NSSGEAALNF PAGEAVVGFS
     TESILDALGG TLDPLLDAIK SGAIKGVVGM VSCTTLRDYG QDVHSVAVVK ELIKRNILVL
     SMGCGNAAMQ VAGLCSPEAR EYAGDSLKAV CEALGVPPVL SYGTCTDTGR LADLLGAISG
     ALGGVPVPDL PVAAAAPEYM EQKATIDAIF ALALGLYTYV NPVPTVTGAP NLVKLLTEDC
     REVTGGLLNV ETDAVKAVDG IEQHIMEKRK KLGI
//