ID   GPD1L_XENLA             Reviewed;         352 AA.
AC   Q801R8;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein;
DE            EC=1.1.1.8;
GN   Name=gpd1l;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-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; BC047958; AAH47958.1; -; mRNA.
DR   EMBL; BC108481; AAI08482.1; -; mRNA.
DR   RefSeq; NP_001080270.1; NM_001086801.1.
DR   AlphaFoldDB; Q801R8; -.
DR   SMR; Q801R8; -.
DR   MaxQB; Q801R8; -.
DR   DNASU; 379962; -.
DR   GeneID; 379962; -.
DR   KEGG; xla:379962; -.
DR   CTD; 379962; -.
DR   Xenbase; XB-GENE-969908; gpd1l.L.
DR   OMA; EMITFAQ; -.
DR   OrthoDB; 476066at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 379962; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] 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; 1.10.1040.10; -; 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   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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03376; glycerol3P_DH; 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_0000286515"
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;  38500 MW;  942B4DAEE369B1EB CRC64;
     MALAGPLKVC IVGSGNWGSA VAKIIGHNVK NMKKFASTVN MWVFEENING RKLTEIINTE
     HENVKYLPGH KLPENVVALP NLTDAVRDAD LLIFVIPHQF IHKVCQEISG KVHKNALGIT
     LIKGIDEGPE GLRLISDIIR EKMNIDVSVL MGANIANEVA AEKFCETTIG SKNKNHGLLF
     KELLQTPNFR ITVVEDADTV ELCGALKNIV AVAAGFCDGL SCGDNTKAAV IRLGLMEMIA
     FANVFCKDSV SIATFLESCG VADLITTCYG GRNRKVAEAF VKTGKSIEEL EKEMLNGQKL
     QGPQTSAEVY RILQQKNMVN NFPLFTAVFQ ICYEGKPVED VISCLQSHPE HM