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G3P2_BACSU
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   03-AUG-2022, entry version 150.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000303|PubMed:10799476};
DE            Short=GAPDH {ECO:0000303|PubMed:10799476};
DE            EC=1.2.1.59 {ECO:0000269|PubMed:10799476};
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:10799476};
GN   Name=gapB {ECO:0000303|PubMed:10799476}; OrderedLocusNames=BSU29020;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(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   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RX   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 physiological
RT   roles in a nonphotosynthetic bacterium.";
RL   J. Biol. Chem. 275:14031-14037(2000).
RN   [4]
RP   INTERACTION WITH BRXC, PTM, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX   PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA   Gaballa A., Su T.T., Helmann J.D.;
RT   "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT   (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL   Redox Biol. 42:101935-101935(2021).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the oxidative
CC       phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-
CC       bisphosphoglycerate (BPG) using the cofactor NADP. The first reaction
CC       step involves the formation of a hemiacetal intermediate between G3P
CC       and a cysteine residue, and this hemiacetal intermediate is then
CC       oxidized to a thioester, with concomitant reduction of NADP to NADPH.
CC       The reduced NADPH is then exchanged with the second NADP, and the
CC       thioester is attacked by a nucleophilic inorganic phosphate to produce
CC       BPG. {ECO:0000269|PubMed:10799476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC         Evidence={ECO:0000269|PubMed:10799476};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC         Evidence={ECO:0000269|PubMed:10799476};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.86 mM for NADP (at pH 9.2 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:10799476};
CC         KM=5.7 mM for NAD (at pH 9.2 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:10799476};
CC         Note=kcat is 1 sec(-1) for dehydrogenase activity with NAD (at pH 9.2
CC         and 25 degrees Celsius). kcat is 8 sec(-1) for dehydrogenase activity
CC         with NADP (at pH 9.2 and 25 degrees Celsius).
CC         {ECO:0000269|PubMed:10799476};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000269|PubMed:10799476}.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with BrxC
CC       (PubMed:33722570). {ECO:0000250|UniProtKB:P00362,
CC       ECO:0000269|PubMed:33722570}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: In response to oxidative stress, the active site Cys likely reacts
CC       with bacillithiol (BSH) to form mixed disulfides to protect the Cys
CC       residue against overoxidation. S-bacillithiolation presumably leads to
CC       loss of catalytic activity. Debacillithiolation by monothiol
CC       bacilliredoxin BrxC restores the activity.
CC       {ECO:0000305|PubMed:33722570}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow in
CC       medium containing asparagine as a sole carbon source but presents the
CC       same growth rate as the wild-type in glucose-containing medium.
CC       {ECO:0000269|PubMed:10799476}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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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; NC_000964.3.
DR   RefSeq; WP_003229459.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34425; -.
DR   SMR; O34425; -.
DR   STRING; 224308.BSU29020; -.
DR   jPOST; O34425; -.
DR   PaxDb; O34425; -.
DR   PRIDE; O34425; -.
DR   EnsemblBacteria; CAB14862; CAB14862; BSU_29020.
DR   GeneID; 937393; -.
DR   KEGG; bsu:BSU29020; -.
DR   PATRIC; fig|224308.179.peg.3151; -.
DR   eggNOG; COG0057; Bacteria.
DR   InParanoid; O34425; -.
DR   OMA; NAKVLAW; -.
DR   PhylomeDB; O34425; -.
DR   BioCyc; BSUB:BSU29020-MON; -.
DR   BRENDA; 1.2.1.13; 658.
DR   BRENDA; 1.2.1.59; 658.
DR   SABIO-RK; O34425; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity; IDA:UniProtKB.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR   GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IMP:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43148; PTHR43148; 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   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Gluconeogenesis; NAD; NADP; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..340
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT                   /id="PRO_0000145635"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         12..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         120
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         151..153
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         182
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         183
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         197
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         210..211
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         233
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         315
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   SITE            179
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GIL8"
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
 
 
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