G3P_SCHMA
ID G3P_SCHMA Reviewed; 338 AA.
AC P20287;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
DE AltName: Full=Major larval surface antigen;
DE AltName: Full=P-37;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=2584935; DOI=10.1084/jem.170.6.2065;
RA Goudot-Crozel V., Caillol D., Djabali M., Dessein A.J.;
RT "The major parasite surface antigen associated with human resistance to
RT schistosomiasis is a 37-kD glyceraldehyde-3P-dehydrogenase.";
RL J. Exp. Med. 170:2065-2080(1989).
CC -!- FUNCTION: This antigen is associated with human resistance to
CC schistosomiasis.
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:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; JL0121; JL0121.
DR RefSeq; XP_018648500.1; XM_018794048.1.
DR PDB; 7JH0; X-ray; 2.51 A; A/B/C/D=1-338.
DR PDBsum; 7JH0; -.
DR AlphaFoldDB; P20287; -.
DR SMR; P20287; -.
DR STRING; 6183.Smp_056970.1; -.
DR PRIDE; P20287; -.
DR EnsemblMetazoa; Smp_056970.2; Smp_056970.2; Smp_056970.
DR GeneID; 8345746; -.
DR KEGG; smm:Smp_056970.1; -.
DR WBParaSite; Smp_056970.2; Smp_056970.2; Smp_056970.
DR CTD; 8345746; -.
DR eggNOG; KOG0657; Eukaryota.
DR OMA; QVKILAW; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P20287; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; PTHR10836; PTHR10836; 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; Glycolysis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145520"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 212..213
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 109..115
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 153..168
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 269..274
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:7JH0"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:7JH0"
FT STRAND 302..315
FT /evidence="ECO:0007829|PDB:7JH0"
FT HELIX 319..337
FT /evidence="ECO:0007829|PDB:7JH0"
SQ SEQUENCE 338 AA; 36378 MW; 3DAC70E93C1E24BE CRC64;
MSRAKVGING FGRIGRLVLR AAFLKNTVDV VSVNDPFIDL EYMVYMIKRD STHGTFPGEV
STENGKLKVN GKLISVHCER DPANIPWDKD GAEYVVESTG VFTTIDKAQA HIKNNRAKKV
IISAPSADAP MFVVGVNENS YEKSMSVVSN ASCTTNCLAP LAKVIHDKFE IVEGLMTTVH
SFTATQKVVD GPSSKLWRDG RGAMQNIIPA STGAAKAVGK VIPALNGKLT GMAFRVPTPD
VSVVDLTCRL GKGASYEEIK AAVKAAASGP LKGILEYTED EVVSSDFVGS TSSSIFDAKA
GISLNNNFVK LVSWYDNEFG YSCRVVDLIT HMHKVDHA
