ID   G3P2_BACSU              Reviewed;         340 AA.
AC   O34425;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 75.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE            EC=1.2.1.59;
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
GN   Name=gapB; OrderedLocusNames=BSU29020;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98048467; PubMed=9387221;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes
RT   in the 200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   CHARACTERIZATION.
RX   MEDLINE=20261518; PubMed=10799476; DOI=10.1074/jbc.275.19.14031;
RA   Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G.,
RA   Aymerich S.;
RT   "Two glyceraldehyde-3-phosphate dehydrogenases with opposite
RT   physiological roles in a nonphotosynthetic bacterium.";
RL   J. Biol. Chem. 275:14031-14037(2000).
CC   -!- FUNCTION: More active in anabolism.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.7 mM for NAD;
CC         KM=0.86 mM for NADP;
CC         Note=The catalytic efficiency is 50-fold higher with NADP than
CC         with NAD;
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; AF008220; AAC00355.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14862.1; -; Genomic_DNA.
DR   PIR; G69628; G69628.
DR   RefSeq; NP_390780.1; -.
DR   HSSP; P00362; 1NQO.
DR   GeneID; 937393; -.
DR   GenomeReviews; AL009126_GR; BSU29020.
DR   KEGG; bsu:BSU29020; -.
DR   NMPDR; fig|224308.1.peg.2905; -.
DR   SubtiList; BG12592; gapB.
DR   HOGENOM; O34425; -.
DR   OMA; O34425; TNPHSAI.
DR   BioCyc; BSUB224308:BSU2898-MON; -.
DR   BRENDA; 1.2.1.59; 150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IEA:EC.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   PANTHER; PTHR10836; GAP_DH; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    340       Glyceraldehyde-3-phosphate dehydrogenase
FT                                2.
FT                                /FTId=PRO_0000145635.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      151    153       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      210    211       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    152    152       Nucleophile (By similarity).
FT   BINDING      78     78       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     182    182       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     197    197       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     233    233       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     315    315       NAD (By similarity).
FT   SITE        179    179       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   340 AA;  37476 MW;  DD1DD4BC7D633EC6 CRC64;
     MKVKVAINGF GRIGRMVFRK AMLDDQIQVV AINASYSAET LAHLIKYDTI HGRYDKEVVA
     GEDSLIVNGK KVLLLNSRDP KQLPWREYDI DIVVEATGKF NAKDKAMGHI EAGAKKVILT
     APGKNEDVTI VMGVNEDQFD AERHVIISNA SCTTNCLAPV VKVLDEEFGI ESGLMTTVHA
     YTNDQKNIDN PHKDLRRARA CGESIIPTTT GAAKALSLVL PHLKGKLHGL ALRVPVPNVS
     LVDLVVDLKT DVTAEEVNEA FKRAAKTSMY GVLDYSDEPL VSTDYNTNPH SAVIDGLTTM
     VMEDRKVKVL AWYDNEWGYS CRVVDLIRHV AARMKHPSAV
//