ID   COOH_RHORU              Reviewed;         361 AA.
AC   P31895;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Carbon monoxide-induced hydrogenase;
GN   Name=cooH;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UR2;
RX   PubMed=8626276; DOI=10.1128/jb.178.6.1515-1524.1996;
RA   Fox J.D., Kerby R.L., Roberts G.P., Ludden P.W.;
RT   "Characterization of the CO-induced, CO-tolerant hydrogenase from
RT   Rhodospirillum rubrum and the gene encoding the large subunit of the
RT   enzyme.";
RL   J. Bacteriol. 178:1515-1524(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-361.
RC   STRAIN=UR1;
RX   PubMed=1644755; DOI=10.1128/jb.174.16.5284-5294.1992;
RA   Kerby R.L., Hong S.S., Ensign S.A., Coppoc L.J., Ludden P.W., Roberts G.P.;
RT   "Genetic and physiological characterization of the Rhodospirillum rubrum
RT   carbon monoxide dehydrogenase system.";
RL   J. Bacteriol. 174:5284-5294(1992).
CC   -!- FUNCTION: The carbon monoxide dehydrogenase (CODH) oxidizes carbon
CC       monoxide coupled, via CooF, to the reduction of a hydrogen cation by a
CC       hydrogenase (probably CooH).
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC   -!- SIMILARITY: To E.coli formate hydrogenlyase hydrogenase isozyme 3 and
CC       to bovine mitochondrial NADH-ubiquinone oxidoreductase. {ECO:0000305}.
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DR   EMBL; U65510; AAC45121.1; -; Genomic_DNA.
DR   PIR; T51319; T51319.
DR   RefSeq; WP_011389179.1; NZ_NHSM01000031.1.
DR   AlphaFoldDB; P31895; -.
DR   SMR; P31895; -.
DR   TCDB; 3.D.1.4.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   OMA; ICSFSHN; -.
DR   BioCyc; MetaCyc:MON-16447; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00346; Complex1_49kDa; 2.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   4: Predicted;
KW   Metal-binding; Nickel; Oxidoreductase.
FT   CHAIN           1..361
FT                   /note="Carbon monoxide-induced hydrogenase"
FT                   /id="PRO_0000090023"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  40280 MW;  130352C4E472A88A CRC64;
     MSTYTIPVGP LHVALEEPMY FRIEVDGEKV VSVDITAGHV HRGIEYLATK RNIYQNIVLT
     ERVCSLCSNS HPQTYCMALE SITGMVVPPR AQYLRVIADE TKRVASHMFN VAILAHIVGF
     DSLFMHVMEA REIMQDTKEA VFGNRMDIAA MAIGGVKYDL DKDGRDYFIG QLDKLEPTLR
     DEIIPLYQTN PSIVDRTRGI GVLSAADCVD YGLMGPVARG SGHAYDVRKQ APYAVYDRLD
     FEMALGEHGD VWSRAMVRWQ EALTSIGLIR QCLRDMPDGP TKAGPVPPIP AGEAVAKTEA
     PRGELIYYLK TNGTDRPERL KWRVPTYMNW DALNVMMAGA RISDIPLIVN SIDPCISCTE
     R