G3P_STRPY
ID G3P_STRPY Reviewed; 336 AA.
AC P0C0G6; P50467; P68776;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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};
DE AltName: Full=Plasmin receptor {ECO:0000303|PubMed:1322883};
DE AltName: Full=Plasminogen-binding protein {ECO:0000303|PubMed:1322883};
GN Name=gap; Synonyms=gapA, plr;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-74; 161-174
RP AND 187-217.
RC STRAIN=64/14;
RX PubMed=1322883; DOI=10.1128/jb.174.16.5204-5210.1992;
RA Lottenberg R., Broder C.C., Boyle M.D., Kain S.J., Schroeder B.L.,
RA Curtiss R. III;
RT "Cloning, sequence analysis, and expression in Escherichia coli of a
RT streptococcal plasmin receptor.";
RL J. Bacteriol. 174:5204-5210(1992).
CC -!- FUNCTION: Also binds human plasminogen.
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 -!- MISCELLANEOUS: Binds human plasminogen. {ECO:0000269|PubMed:1322883}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M95569; AAA26953.1; -; Genomic_DNA.
DR RefSeq; WP_014635277.1; NZ_WVFT01000010.1.
DR PDB; 6ITE; X-ray; 1.74 A; O/P/Q/R=1-336.
DR PDBsum; 6ITE; -.
DR AlphaFoldDB; P0C0G6; -.
DR SMR; P0C0G6; -.
DR PRIDE; P0C0G6; -.
DR GeneID; 57852064; -.
DR eggNOG; COG0057; Bacteria.
DR BRENDA; 1.2.1.12; 5935.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:CAFA.
DR GO; GO:0051287; F:NAD binding; IDA:CAFA.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0002020; F:protease binding; IDA:CAFA.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006735; P:NADH regeneration; IDA:CAFA.
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; Direct protein sequencing; Glycolysis; NAD;
KW Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1322883"
FT CHAIN 2..336
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145703"
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:6ITE"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:6ITE"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6ITE"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6ITE"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6ITE"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6ITE"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6ITE"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:6ITE"
FT HELIX 318..334
FT /evidence="ECO:0007829|PDB:6ITE"
SQ SEQUENCE 336 AA; 35959 MW; 7EF52109AAE7F6B7 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 SAMKAASNDS FGYTEDPIVS SDIVGVSYGS LFDATQTKVM
EVDGSQLVKV VSWYDNEMSY TAQLVRTLEY FAKIAK
