ID G3P_CORGL Reviewed; 334 AA.
AC Q01651;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83};
DE Short=GAPDH {ECO:0000250|UniProtKB:P9WN83};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P9WN83};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83};
GN Name=gap; OrderedLocusNames=Cgl1588, cg1791;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=1400158; DOI=10.1128/jb.174.19.6076-6086.1992;
RA Eikmanns B.J.;
RT "Identification, sequence analysis, and expression of a Corynebacterium
RT glutamicum gene cluster encoding the three glycolytic enzymes
RT glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and
RT triosephosphate isomerase.";
RL J. Bacteriol. 174:6076-6086(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC NAD. The first reaction step involves the formation of a hemiacetal
CC intermediate between G3P and a cysteine residue, and this hemiacetal
CC intermediate is then oxidized to a thioester, with concomitant
CC reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC second NAD, and the thioester is attacked by a nucleophilic inorganic
CC phosphate to produce BPG. {ECO:0000250|UniProtKB:P9WN83}.
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:0000250|UniProtKB:P9WN83};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P54226}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X59403; CAA42045.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98981.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21596.1; -; Genomic_DNA.
DR PIR; A43260; A43260.
DR RefSeq; NP_600802.1; NC_003450.3.
DR RefSeq; WP_003862250.1; NC_006958.1.
DR PDB; 8HRO; X-ray; 2.59 A; A/B=1-334.
DR PDB; 8HRP; X-ray; 1.99 A; A/B/C/D/E/F/G/H=1-334.
DR PDB; 8HRQ; X-ray; 2.09 A; A/B=1-334.
DR PDB; 8HRR; X-ray; 2.00 A; A/B=1-334.
DR PDB; 8HRS; X-ray; 2.00 A; A/B/C/D=1-334.
DR PDBsum; 8HRO; -.
DR PDBsum; 8HRP; -.
DR PDBsum; 8HRQ; -.
DR PDBsum; 8HRR; -.
DR PDBsum; 8HRS; -.
DR AlphaFoldDB; Q01651; -.
DR SMR; Q01651; -.
DR STRING; 196627.cg1791; -.
DR World-2DPAGE; 0001:Q01651; -.
DR KEGG; cgb:cg1791; -.
DR KEGG; cgl:Cgl1588; -.
DR PATRIC; fig|196627.13.peg.1550; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_11; -.
DR OrthoDB; 9803304at2; -.
DR BioCyc; CORYNE:G18NG-11173-MONOMER; -.
DR BRENDA; 1.2.1.12; 960.
DR BRENDA; 1.2.1.59; 960.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145647"
FT ACT_SITE 153
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 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 198
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 234
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 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT CONFLICT 25..26
FT /note="SD -> NG (in Ref. 1; CAA42045)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..334
FT /note="KL -> QALN (in Ref. 1; CAA42045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36046 MW; 33792AF65FA90FA7 CRC64;
MTIRVGINGF GRIGRNFFRA VLERSDDLEV VAVNDLTDNK TLSTLLKFDS IMGRLGQEVE
YDDDSITVGG KRIAVYAERD PKNLDWAAHN VDIVIESTGF FTDANAAKAH IEAGAKKVII
SAPASNEDAT FVYGVNHESY DPENHNVISG ASCTTNCLAP MAKVLNDKFG IENGLMTTVH
AYTGDQRLHD APHRDLRRAR AAAVNIVPTS TGAAKAVALV LPELKGKLDG YALRVPVITG
SATDLTFNTK SEVTVESINA AIKEAAVGEF GETLAYSEEP LVSTDIVHDS HGSIFDAGLT
KVSGNTVKVV SWYDNEWGYT CQLLRLTELV ASKL
//
