ID Q37322_EUGGR Unreviewed; 460 AA.
AC Q37322;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
DE Flags: Precursor;
GN Name=gapA {ECO:0000313|EMBL:AAD10216.1};
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039 {ECO:0000313|EMBL:AAD10216.1};
RN [1] {ECO:0000313|EMBL:AAD10216.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SAG 1224-5/25 {ECO:0000313|EMBL:AAD10216.1};
RX PubMed=7568085; DOI=10.1073/pnas.92.20.9122;
RA Henze K., Badr A., Wettern M., Cerff R., Martin W.;
RT "A nuclear gene of eubacterial origin in Euglena gracilis reflects cryptic
RT endosymbioses during protist evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9122-9126(1995).
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:0000256|RuleBase:RU361160};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00035876};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000256|ARBA:ARBA00005215}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|RuleBase:RU361160}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; L21904; AAD10216.1; -; mRNA.
DR AlphaFoldDB; Q37322; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Glycolysis {ECO:0000256|RuleBase:RU361160};
KW NAD {ECO:0000256|RuleBase:RU361160};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 127..278
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 460 AA; 48599 MW; 8C5729FDB772F9F1 CRC64;
MAVGSSMSAT TQMHVQPAVR ATTRVQPTLA MRGQISRLAA NSQVYAEAPA AYEFQAPAQA
SGVSSGIAAM VMAPVAAAAA FFAYKKGQSD AQTYEVADPA GVQTYGTELV FAMNATIGNK
YPGNSNTKAA ISGFGRIGRN VLRCWYGRNP KPFDIVAINA GSMSPEQAAH LLKYDSVLGT
FEADVQYGDD WISVDGKKLK LLTTRDPAQA PWKELGVEIV IEGTGAFNSL DGSSKHLTAG
AKKVVITAPG KNCPTYVCGV NEDQYNPATD HVISNASCTT NGMAGVCKVL DENFTVQYGT
MTTTHSYTGD QMILDGRHSD LRRARAGAVN IVPTSTGAAK AVALVLPNLK GKLNGIALRV
PTPNVSIVDL VVKVDKKTTK EEVNAALKKA ADGPLNGVLG YTELPLVSSD FKGTNVSATV
DGQLSMVMGE DMVKVVMWYD NEWGYSQRVV DLTAVVAGKL
//
