G3P1_BACSU
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 03-AUG-2022, entry version 167.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1 {ECO:0000303|PubMed:10799476};
DE Short=GAPDH {ECO:0000303|PubMed:10799476};
DE EC=1.2.1.12 {ECO:0000269|PubMed:10799476};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:10799476};
GN Name=gapA {ECO:0000303|PubMed:10799476}; Synonyms=gap;
GN OrderedLocusNames=BSU33940;
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 / BD170;
RX 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 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 2-31.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
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 PubMed=10658653; DOI=10.1099/00221287-146-1-65;
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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND INDUCTION.
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 [6]
RP TRANSCRIPTIONAL REGULATION BY CGGR.
RC STRAIN=168;
RX PubMed=12622823; DOI=10.1046/j.1365-2958.2003.03404.x;
RA Doan T., Aymerich S.;
RT "Regulation of the central glycolytic genes in Bacillus subtilis: binding
RT of the repressor CggR to its single DNA target sequence is modulated by
RT fructose-1,6-bisphosphate.";
RL Mol. Microbiol. 47:1709-1721(2003).
RN [7]
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 glycolysis. Catalyzes the oxidative
CC phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-
CC bisphosphoglycerate (BPG) using the cofactor NAD. 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 NAD to NADH. The
CC reduced NADH is then exchanged with the second NAD, and the thioester
CC is attacked by a nucleophilic inorganic phosphate to produce BPG.
CC {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=1.2.1.12;
CC Evidence={ECO:0000269|PubMed:10799476};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {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:0000269|PubMed:10658653}.
CC -!- INDUCTION: Repressed by CggR and indirectly stimulated by CcpA.
CC {ECO:0000269|PubMed:10799476, ECO:0000269|PubMed:12622823}.
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 glucose as a sole carbon source but presents the same
CC growth rate as the wild-type in asparagine-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; X13011; CAA31434.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15399.1; -; Genomic_DNA.
DR PIR; S02754; DEBSG.
DR RefSeq; NP_391274.1; NC_000964.3.
DR RefSeq; WP_003219957.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P09124; -.
DR SMR; P09124; -.
DR IntAct; P09124; 2.
DR MINT; P09124; -.
DR STRING; 224308.BSU33940; -.
DR jPOST; P09124; -.
DR PaxDb; P09124; -.
DR PRIDE; P09124; -.
DR EnsemblBacteria; CAB15399; CAB15399; BSU_33940.
DR GeneID; 64305160; -.
DR GeneID; 938627; -.
DR KEGG; bsu:BSU33940; -.
DR PATRIC; fig|224308.179.peg.3680; -.
DR eggNOG; COG0057; Bacteria.
DR InParanoid; P09124; -.
DR OMA; HETYKGE; -.
DR PhylomeDB; P09124; -.
DR BioCyc; BSUB:BSU33940-MON; -.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P09124; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:UniProtKB.
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; Direct protein sequencing; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10658653,
FT ECO:0000269|PubMed:8755892"
FT CHAIN 2..335
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000145634"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT CONFLICT 5
FT /note="V -> VI (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
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
