ID   G3P1_BACSU              Reviewed;         335 AA.
AC   P09124;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 86.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            EC=1.2.1.12;
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
GN   Name=gapA; Synonyms=gap; OrderedLocusNames=BSU33940;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BD170;
RX   MEDLINE=89160255; PubMed=2493629; DOI=10.1093/nar/17.3.1251;
RA   Viaene A., Dhaese P.;
RT   "Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from
RT   Bacillus subtilis.";
RL   Nucleic Acids Res. 17:1251-1251(1989).
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   PROTEIN SEQUENCE OF 2-31.
RC   STRAIN=168 / JH642;
RX   MEDLINE=96345629; PubMed=8755892;
RA   Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT   "Cold shock stress-induced proteins in Bacillus subtilis.";
RL   J. Bacteriol. 178:4611-4619(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-12, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   MEDLINE=20121740; PubMed=10658653;
RA   Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT   "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT   dimensional protein electrophoretic study.";
RL   Microbiology 146:65-75(2000).
RN   [5]
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 catabolism.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X13011; CAA31434.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15399.1; -; Genomic_DNA.
DR   PIR; S02754; DEBSG.
DR   RefSeq; NP_391274.1; -.
DR   HSSP; P00362; 1NQO.
DR   SMR; P09124; 2-335.
DR   PhosSite; P09124; -.
DR   GeneID; 938627; -.
DR   GenomeReviews; AL009126_GR; BSU33940.
DR   KEGG; bsu:BSU33940; -.
DR   NMPDR; fig|224308.1.peg.3400; -.
DR   SubtiList; BG10827; gapA.
DR   HOGENOM; P09124; -.
DR   OMA; P09124; YDSTFGV.
DR   BioCyc; BSUB224308:BSU3391-MON; -.
DR   BRENDA; 1.2.1.12; 150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:EC.
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   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; Direct protein sequencing; Glycolysis;
KW   NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    335       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145634.
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      34     34       NAD (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).
FT   CONFLICT      5      5       V -> VI (in Ref. 4; AA sequence).
SQ   SEQUENCE   335 AA;  35833 MW;  B7A422A5CE3AD1DF CRC64;
     MAVKVGINGF GRIGRNVFRA ALNNPEVEVV AVNDLTDANM LAHLLQYDSV HGKLDAEVSV
     DGNNLVVNGK TIEVSAERDP AKLSWGKQGV EIVVESTGFF TKRADAAKHL EAGAKKVIIS
     APANEEDITI VMGVNEDKYD AANHDVISNA SCTTNCLAPF AKVLNDKFGI KRGMMTTVHS
     YTNDQQILDL PHKDYRRARA AAENIIPTST GAAKAVSLVL PELKGKLNGG AMRVPTPNVS
     LVDLVAELNQ EVTAEEVNAA LKEAAEGDLK GILGYSEEPL VSGDYNGNKN SSTIDALSTM
     VMEGSMVKVI SWYDNESGYS NRVVDLAAYI AKKGL
//