ID   G3PC_CHOCR              Reviewed;         335 AA.
AC   P34920;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC;
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Stackhouse;
RX   PubMed=8007000; DOI=10.1007/bf00163149;
RA   Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B., Cerff R.;
RT   "The evolutionary origin of red algae as deduced from the nuclear genes
RT   encoding cytosolic and chloroplast glyceraldehyde-3-phosphate
RT   dehydrogenases from Chondrus crispus.";
RL   J. Mol. Evol. 38:319-327(1994).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X73034; CAA51515.1; -; mRNA.
DR   EMBL; X73036; CAA51517.1; -; Genomic_DNA.
DR   PIR; S43339; S43339.
DR   AlphaFoldDB; P34920; -.
DR   SMR; P34920; -.
DR   PRIDE; P34920; -.
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..335
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT                   /id="PRO_0000145597"
FT   ACT_SITE        152
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         151..153
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         211..212
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            179
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        250
FT                   /note="A -> T (in Ref. 1; CAA51517)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  36054 MW;  B09241EF399D397C CRC64;
     MTAPKVGING FGRIGRLVLR AAIEKGTCQV VAINDPFIDL DYMAYMLKYD STHGRYAGDV
     SIKDGKLQVD GNSITVFAHR DPAEIPWATA AADYIVEATG VFTLKDKAAA HFKGGAKKVV
     ISAPSKDAPM FVCGVNEAKY TPDLDIISNA SCTTNCLAPL VKVIHEKYGI EEGLMTTVHA
     TTATQKTVDG PSNKDWRGGR GRGRNIIPSS TGAAKAVGKV MPELNGKLTG MAFRVPTPDV
     SVVDLTVRLA SETTYEDIKA TMKAAADDSM KGIMKYTEDA VVSTDFIHDD ASCIFDASAG
     IMLNSKFCKL VAWYDNEWGY SNRVVDLIAH ISKVQ