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 03-AUG-2022, entry version 127.
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}.
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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 AlphaFoldDB; P80869; -.
DR SMR; P80869; -.
DR STRING; 224308.BSU02830; -.
DR PaxDb; P80869; -.
DR PRIDE; P80869; -.
DR EnsemblBacteria; CAB12077; CAB12077; BSU_02830.
DR GeneID; 938377; -.
DR KEGG; bsu:BSU02830; -.
DR PATRIC; fig|224308.179.peg.294; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P80869; -.
DR OMA; MTLYPSQ; -.
DR PhylomeDB; P80869; -.
DR BioCyc; BSUB:BSU02830-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047934; F:glucose 1-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:RHEA.
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 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;
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 ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="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
