(data stored in SCRATCH zone)

SWISSPROT: DHG2_BACSU

ID   DHG2_BACSU              Reviewed;         258 AA.
AC   P80869;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=Glucose 1-dehydrogenase 2;
DE            EC=1.1.1.47;
DE   AltName: Full=GLCDH-II;
DE            Short=GDH-II;
DE   AltName: Full=General stress protein 74;
DE            Short=GSP74;
GN   Name=ycdF; OrderedLocusNames=BSU02830;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274031; DOI=10.1099/00221287-143-8-2775;
RA   Kumano M., Tamakoshi A., Yamane K.;
RT   "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT   gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT   identification of the site of the lin-2 mutation.";
RL   Microbiology 143:2775-2782(1997).
RN   [2]
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-13.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH;
CC         Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation and oxygen limitation.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
DR   EMBL; AB000617; BAA22244.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12077.1; -; Genomic_DNA.
DR   PIR; G69755; G69755.
DR   RefSeq; NP_388165.1; NC_000964.3.
DR   RefSeq; WP_003246415.1; NZ_JNCM01000030.1.
DR   SMR; P80869; -.
DR   STRING; 224308.BSU02830; -.
DR   PaxDb; P80869; -.
DR   PRIDE; P80869; -.
DR   EnsemblBacteria; CAB12077; CAB12077; BSU02830.
DR   GeneID; 938377; -.
DR   KEGG; bsu:BSU02830; -.
DR   PATRIC; fig|224308.179.peg.294; -.
DR   eggNOG; ENOG4105H9W; Bacteria.
DR   eggNOG; COG1028; LUCA.
DR   InParanoid; P80869; -.
DR   KO; K00034; -.
DR   OMA; MTLYPSQ; -.
DR   PhylomeDB; P80869; -.
DR   BioCyc; BSUB:BSU02830-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0055114; P:oxidation-reduction 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   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P80869.
DR   SWISS-2DPAGE; P80869.
KW   Direct protein sequencing; NADP; Oxidoreductase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..258
FT                   /note="Glucose 1-dehydrogenase 2"
FT                   /id="PRO_0000054617"
FT   NP_BIND         11..35
FT                   /note="NADP"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         146
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   258 AA;  27776 MW;  77842DC45D496C26 CRC64;
     MYKDLTGKTA IVTGSSKGIG KAIAERFGKE KMNVVVNYHS DPSGADETLE IIKQNGGKAV
     SVEADVSKEE GIQALLDTAL EHFGTLDVMV NNSGFNGVEA MPHEMSLEDW QRVIDVNVTG
     TFLGAKAALN HMMKNNIKGN VLNISSVHQQ IPRPVNVQYS TSKGGIKMMT ETLALNYADK
     GIRVNAIAPG TIATESNVDT KKEESRQKQL KKIPMKAFGK PEEVAAAAAW LVSEEASYVT
     GATLFVDGGM TLYPSQLE
//

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