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Database: UniProt
Entry: S5LRB0_9CARY
LinkDB: S5LRB0_9CARY
Original site: S5LRB0_9CARY 
ID   S5LRB0_9CARY            Unreviewed;       187 AA.
AC   S5LRB0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AGR28090.1};
DE            EC=1.2.1.12 {ECO:0000313|EMBL:AGR28090.1};
DE   Flags: Fragment;
GN   Name=GAPC {ECO:0000313|EMBL:AGR28090.1};
OS   Delosperma litorale.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Delosperma.
OX   NCBI_TaxID=1346866 {ECO:0000313|EMBL:AGR28090.1};
RN   [1] {ECO:0000313|EMBL:AGR28090.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rohwer A., Pekovich S., Strohmeyer R.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406}.
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DR   EMBL; KF227898; AGR28090.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5LRB0; -.
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   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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF112; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2, CYTOSOLIC; 1.
DR   Pfam; PF02800; Gp_dh_C; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AGR28090.1}.
FT   DOMAIN          1..47
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGR28090.1"
FT   NON_TER         187
FT                   /evidence="ECO:0000313|EMBL:AGR28090.1"
SQ   SEQUENCE   187 AA;  19758 MW;  2FE56E6432EF1CE7 CRC64;
     EKAAAHLKGG AKKVVISAPS KDAPMFVVGV NEKEYKPELN IVSNASCTTN CLATLAKVIN
     DRFGIVEGLM TTIHSITASQ KTVDGPSNKD WRGGRAASFN IIPSSTGAAK AVGKVLPVLN
     GKLTGMSFRV PTIDVSVVDL TVRLEKAATY EDIKAAMKEE SEGNLKGILG YTEEDVVSTD
     FIGDSRS
//
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