ID   G3PC_COEVA              Reviewed;         312 AA.
AC   Q8VXQ8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
DE   Flags: Fragment;
GN   Name=GapC;
OS   Coelastrella vacuolata (Green alga) (Chlorella fusca var. vacuolata).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Scenedesmus.
OX   NCBI_TaxID=77546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=SAG 211-8b;
RX   PubMed=15830207; DOI=10.1007/s00425-005-1501-0;
RA   Valverde F., Ortega J.M., Losada M., Serrano A.;
RT   "Sugar-mediated transcriptional regulation of the Gap gene system and
RT   concerted photosystem II functional modulation in the microalga Scenedesmus
RT   vacuolatus.";
RL   Planta 221:937-952(2005).
CC   -!- FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the
CC       pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-
CC       phospho-D-glyceroyl phosphate. Essential for the maintenance of
CC       cellular ATP levels and carbohydrate metabolism (By similarity).
CC       {ECO:0000250}.
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   -!- INDUCTION: Induced by sugar addition. {ECO:0000269|PubMed:15830207}.
CC   -!- MISCELLANEOUS: Algae contain three forms of GAPDH: two cytosolic forms
CC       which participate in glycolysis and one chloroplastic form which
CC       participates in photosynthesis. These three forms are encoded by
CC       distinct genes.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ252209; CAC81012.1; -; mRNA.
DR   AlphaFoldDB; Q8VXQ8; -.
DR   SMR; Q8VXQ8; -.
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..>312
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT                   /id="PRO_0000292346"
FT   ACT_SITE        145
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         5..6
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..146
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..205
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            172
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         312
SQ   SEQUENCE   312 AA;  33249 MW;  7DBF8B7F4BBC8219 CRC64;
     NGFGRIGSLV LRATLDRKDV KVVAINDPFI EGEYMAYMFK YDSVHGRYEG DVQGDKHGIT
     INGEQIKTLA MMDPTQIPWG EVGADYVVES TGVFTTVDKC QAHLKGGAKK VVISAPSADA
     PMFVMGVNAD KYDPKQHTVV SNASCTTNCL APLAKVVNDT FGIKEALMTT VHATTATQKT
     VDGPSKKDWR GGRGASANII PSSTGAAKAV GKVIPELNGK LTGMAFRVPT QDVSVVDLTC
     ILEKPAKYED IMAALKAASE GPMKGILGYT EDDVVSSDFV SDPASSTVDA KAGIMLSPTF
     VKLVSWYDNE WG