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HOXU_RHOOP
ID   HOXU_RHOOP              Reviewed;          33 AA.
AC   P22659;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=NAD-reducing hydrogenase HoxS subunit gamma;
DE            EC=1.12.1.2;
DE   Flags: Fragment;
GN   Name=hoxU;
OS   Rhodococcus opacus (Nocardia opaca).
OG   Plasmid.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=37919;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=1B;
RX   PubMed=2496982; DOI=10.1111/j.1432-1033.1989.tb14708.x;
RA   Zaborosch C., Schneider K., Schlegel H.G., Kratzin H.;
RT   "Comparison of the NH2-terminal amino acid sequences of the four non-
RT   identical subunits of the NAD-linked hydrogenases from Nocardia opaca 1b
RT   and Alcaligenes eutrophus H16.";
RL   Eur. J. Biochem. 181:175-180(1989).
CC   -!- FUNCTION: Subunits alpha and gamma of HoxS constitute an NADH--
CC       oxidoreductase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2 + NAD(+) = H(+) + NADH; Xref=Rhea:RHEA:24636,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.12.1.2;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Tetramer of an alpha and a gamma subunits (flavin-containing
CC       dimer), and a delta and a nickel-containing beta subunits (hydrogenase
CC       dimer).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P22659; -.
DR   SMR; P22659; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047985; F:hydrogen dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   SUPFAM; SSF54292; SSF54292; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 4Fe-4S; Cytoplasm; Direct protein sequencing; Flavoprotein; FMN;
KW   Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..>33
FT                   /note="NAD-reducing hydrogenase HoxS subunit gamma"
FT                   /id="PRO_0000118539"
FT   DOMAIN          1..>33
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   NON_TER         33
SQ   SEQUENCE   33 AA;  3492 MW;  62AF6E43F64E719D CRC64;
     SIEIEIDGVT VTTEESRTLV DVAAEAGVYI PTL
 
 
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