G3P_STRP8
ID G3P_STRP8 Reviewed; 336 AA.
AC P68777; P50467;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
GN Name=gap; Synonyms=gapA, plr; OrderedLocusNames=spyM18_0261;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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:P00362}.
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:P09124};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00362}.
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; AE009949; AAL97041.1; -; Genomic_DNA.
DR RefSeq; WP_002986042.1; NC_003485.1.
DR PDB; 6FZH; X-ray; 1.50 A; A/B=1-336.
DR PDBsum; 6FZH; -.
DR AlphaFoldDB; P68777; -.
DR SMR; P68777; -.
DR MoonProt; P68777; -.
DR KEGG; spm:spyM18_0261; -.
DR HOGENOM; CLU_030140_0_3_9; -.
DR OMA; NCVAPMA; -.
DR UniPathway; UPA00109; UER00184.
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 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 3D-structure; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..336
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145707"
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 121
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 199
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 212..213
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 235
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 316
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 STRAND 3..8
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:6FZH"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6FZH"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6FZH"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6FZH"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6FZH"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:6FZH"
FT HELIX 318..334
FT /evidence="ECO:0007829|PDB:6FZH"
SQ SEQUENCE 336 AA; 35943 MW; DF15211F663DE07B CRC64;
MVVKVGINGF GRIGRLAFRR IQNIEGVEVT RINDLTDPNM LAHLLKYDTT QGRFDGTVEV
KEGGFEVNGN FIKVSAERDP ENIDWATDGV EIVLEATGFF AKKEAAEKHL HANGAKKVVI
TAPGGNDVKT VVFNTNHDIL DGTETVISGA SCTTNCLAPM AKALHDAFGI QKGLMTTIHA
YTGDQMILDG PHRGGDLRRA RAGAANIVPN STGAAKAIGL VIPELNGKLD GAAQRVPVPT
GSVTELVVTL DKNVSVDEIN AAMKAASNDS FGYTEDPIVS SDIVGVSYGS LFDATQTKVM
EVDGSQLVKV VSWYDNEMSY TAQLVRTLEY FAKIAK
