ID   GPD1L_XENTR             Reviewed;         352 AA.
AC   Q6P824;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein;
DE            EC=1.1.1.8;
GN   Name=gpd1l;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in regulating cardiac sodium current.
CC       {ECO:0000250|UniProtKB:Q8N335}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC         Evidence={ECO:0000250|UniProtKB:Q8N335};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC         Evidence={ECO:0000250|UniProtKB:Q8N335};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; BC061407; AAH61407.1; -; mRNA.
DR   RefSeq; NP_989027.1; NM_203696.1.
DR   AlphaFoldDB; Q6P824; -.
DR   SMR; Q6P824; -.
DR   STRING; 8364.ENSXETP00000022012; -.
DR   PaxDb; 8364-ENSXETP00000032859; -.
DR   DNASU; 394623; -.
DR   Ensembl; ENSXETT00000032859; ENSXETP00000032859; ENSXETG00000015022.
DR   Ensembl; ENSXETT00000123565; ENSXETP00000113270; ENSXETG00000015022.
DR   GeneID; 394623; -.
DR   KEGG; xtr:394623; -.
DR   AGR; Xenbase:XB-GENE-969902; -.
DR   CTD; 23171; -.
DR   Xenbase; XB-GENE-969902; gpd1l.
DR   eggNOG; KOG2711; Eukaryota.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   InParanoid; Q6P824; -.
DR   OMA; EMITFAQ; -.
DR   OrthoDB; 3675564at2759; -.
DR   PhylomeDB; Q6P824; -.
DR   TreeFam; TF300836; -.
DR   Reactome; R-XTR-1483166; Synthesis of PA.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Bgee; ENSXETG00000015022; Expressed in embryo and 13 other cell types or tissues.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF7; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1-LIKE PROTEIN; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Glycerol-3-phosphate dehydrogenase 1-like protein"
FT                   /id="PRO_0000286516"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         272..273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  38464 MW;  2E08E289DCF0A934 CRC64;
     MALAGPLKVC IVGSGNWGSA VAKIIGHNVK NLKKFASTVN MWVFEENING RKLTEIINTE
     HENVKYLPGY KLPENVVAVP NLSDAVKDAD LLIFVIPHQF IHKICQEISG KVHRNALGIT
     LIKGIDEGPE GLRLISDIIR EKMDIDVSVL MGANIANEVA AEKFCETTIG SKNKEHGLLF
     KELLQTPNFR ITVVEDADTV ELCGALKNIV AVAAGFCDGL GCGDNTKAAV IRLGLMEMIA
     FANVFCKGPV SIATFLESCG VADLITTCYG GRNRKVSEAF VKSGKSIEEL EKEMLNGQKL
     QGPQTSAEVY RILQQKNMVN KFPLFTAVYQ ICYEGKPVED VISCLQSHPE HM
//