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BZRD_BACSU
ID   BZRD_BACSU              Reviewed;         243 AA.
AC   O32099;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Benzil reductase ((S)-benzoin forming);
DE            EC=1.1.1.320;
GN   Name=yueD; OrderedLocusNames=BSU31840;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Reduces benzil stereospecifically to (S)-benzoin.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-benzoin + NADP(+) = benzil + H(+) + NADPH;
CC         Xref=Rhea:RHEA:25968, ChEBI:CHEBI:15378, ChEBI:CHEBI:51507,
CC         ChEBI:CHEBI:51510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.320;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB15172.1; -; Genomic_DNA.
DR   PIR; E70007; E70007.
DR   RefSeq; NP_391062.1; NC_000964.3.
DR   RefSeq; WP_003244421.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32099; -.
DR   SMR; O32099; -.
DR   STRING; 224308.BSU31840; -.
DR   PaxDb; O32099; -.
DR   PRIDE; O32099; -.
DR   EnsemblBacteria; CAB15172; CAB15172; BSU_31840.
DR   GeneID; 936558; -.
DR   KEGG; bsu:BSU31840; -.
DR   PATRIC; fig|224308.179.peg.3450; -.
DR   eggNOG; COG1028; Bacteria.
DR   InParanoid; O32099; -.
DR   OMA; PYKGWSA; -.
DR   PhylomeDB; O32099; -.
DR   BioCyc; BSUB:BSU31840-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102306; F:benzil reductase [(S)-benzoin-forming] activity; IEA:UniProtKB-EC.
DR   GO; GO:0004757; F:sepiapterin reductase activity; IBA:GO_Central.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..243
FT                   /note="Benzil reductase ((S)-benzoin forming)"
FT                   /id="PRO_0000366976"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         5..27
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   243 AA;  27109 MW;  65C51BBE5559FB13 CRC64;
     MELYIITGAS KGLGQAIALQ ALEKGHEVHA LSRTKTDVSH KKLTQHQIDL INLEEAEQQF
     ETLLSSIDSD RYSGITLINN AGMVTPIKRA GEASLDELQR HYQLNLTAPV LLSQLFTKRF
     ASYSGKKTVV NITSGAAKNP YKGWSAYCSS KAGLDMFTRT FGFEQEDEEL PVNMISFSPG
     VMDTEMQAVI RSSSKKDFHH IERFRKLNET GSLRSPDFIA GTLLSLLEKG TENGRIYDIK
     EFL
 
 
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