G3P1_GLORO
ID G3P1_GLORO Reviewed; 324 AA.
AC O16027;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE Short=GAPDH-1;
DE EC=1.2.1.12;
DE Flags: Fragment;
GN Name=GPD-1;
OS Globodera rostochiensis (Golden nematode worm) (Heterodera rostochiensis).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=31243;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Ro1 / Mierenbos;
RX PubMed=9851607; DOI=10.1016/s0166-6851(98)00108-x;
RA Qin L., Smant G., Stokkermans J.P.W.G., Bakker J., Schots A., Helder J.;
RT "Cloning of a trans-spliced glyceraldehyde-3-phosphate-dehydrogenase gene
RT from the potato cyst nematode Globodera rostochiensis and expression of its
RT putative promoter region in Caenorhabditis elegans.";
RL Mol. Biochem. Parasitol. 96:59-67(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AF004522; AAC79129.1; -; mRNA.
DR AlphaFoldDB; O16027; -.
DR SMR; O16027; -.
DR PRIDE; O16027; -.
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; 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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN 1..>324
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000145516"
FT ACT_SITE 158
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 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 157..159
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 217..218
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT NON_TER 324
SQ SEQUENCE 324 AA; 34580 MW; 1815C606CBBE1039 CRC64;
MVKPKVGING FGRIGRLALR AAVEKDTVQV VAINDPFIEL DYMVYMFNYD STHGRFNGKI
STSAGNLVVE KEGKATHTIK VFNLKDPAEI KWAEVGAEYV IESTGVFTTI EKASAHLKGG
AKKVVISAPS ADAPMYVMGV NEDKYDPAKD NVISNASCTT NCLAPLAKVI NDEFGIIEGL
MTTVHAVTAT QKTVDGPNGK QWRDGRGAAQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR
VPTPNVSVVD LTARLEKPAS LDAIKAAVKK AAEGNLKGIL GYTEDQVVST DFLGDSRSSI
FDAGACISLN PHFVKLVSWY DNEF
