G3P_ONCVO
ID G3P_ONCVO Reviewed; 339 AA.
AC O01360; O01656;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
DE AltName: Full=Larval antigen OvB95;
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schneider E.A., Gallin M.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Forest;
RA Joseph G.T., Huima T., Lustigman S.;
RT "Onchocerca volvulus: molecular cloning and characterization of a larval
RT antigen, OvB95 recognized by putatively immune individuals from Liberia and
RT Ecuador.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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}.
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 EMBL; Y09455; CAA70607.1; -; mRNA.
DR EMBL; U96177; AAB52599.1; -; mRNA.
DR AlphaFoldDB; O01360; -.
DR SMR; O01360; -.
DR STRING; 6282.O01360; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000024404; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..339
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145519"
FT ACT_SITE 157
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 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 156..158
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 216..217
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 108
FT /note="H -> T (in Ref. 2; AAB52599)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="S -> F (in Ref. 2; AAB52599)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="H -> Y (in Ref. 2; AAB52599)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="C -> R (in Ref. 2; AAB52599)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="V -> I (in Ref. 2; AAB52599)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="N -> I (in Ref. 2; AAB52599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 36180 MW; 5BC933D05FD49B16 CRC64;
MSKPKIGING FGRIGRLVLR AAVEKDTVEV VAVNDPFINI DYMVYMFKYD STHGRFKGHV
SAEGGKLIVT NGKTTHQIAV HNSKDPAEIP WGVEGAEYVV ESTGVFTHTE KASAHLKGGA
KKVIISAPSA DAPMFVMGVN NDKYDKANNH IISNASCTTN CLAPLAKVIH DKFGIIEGLM
TTVHATTATQ KTVDGPSGKL WRDGRGAGQN IIPASTGAAK AVGKVIPDLN GKLTGMASRV
PTPDVSVVDL TCRLQKGASM DEIKAAVKEA AAGPMKGILE YTEDQVVSSD FVGDPHSSIF
DALACISLNP NFVKLIAWYD NEYGYSNRVV DLISYNASK
