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 27-MAR-2024, entry version 156.
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; Bacillota; 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; 224308-BSU29020; -.
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 OrthoDB; 9803304at2; -.
DR PhylomeDB; O34425; -.
DR BioCyc; BSUB:BSU29020-MONOMER; -.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
