ID   GPD1L_DANRE             Reviewed;         351 AA.
AC   Q5XIZ6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein;
DE            EC=1.1.1.8;
GN   Name=gpd1l;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) 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; BC083522; AAH83522.1; -; mRNA.
DR   RefSeq; NP_001005934.1; NM_001005934.1.
DR   RefSeq; XP_009290808.1; XM_009292533.2.
DR   AlphaFoldDB; Q5XIZ6; -.
DR   SMR; Q5XIZ6; -.
DR   STRING; 7955.ENSDARP00000123149; -.
DR   PaxDb; Q5XIZ6; -.
DR   Ensembl; ENSDART00000058550; ENSDARP00000058549; ENSDARG00000040024.
DR   Ensembl; ENSDART00000133642; ENSDARP00000123149; ENSDARG00000040024.
DR   GeneID; 449663; -.
DR   KEGG; dre:449663; -.
DR   CTD; 23171; -.
DR   ZFIN; ZDB-GENE-041010-220; gpd1l.
DR   eggNOG; KOG2711; Eukaryota.
DR   GeneTree; ENSGT00390000003114; -.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   InParanoid; Q5XIZ6; -.
DR   OMA; FIHKVCD; -.
DR   OrthoDB; 476066at2759; -.
DR   PhylomeDB; Q5XIZ6; -.
DR   TreeFam; TF300836; -.
DR   Reactome; R-DRE-1483166; Synthesis of PA.
DR   PRO; PR:Q5XIZ6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000040024; Expressed in early embryo and 25 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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..351
FT                   /note="Glycerol-3-phosphate dehydrogenase 1-like protein"
FT                   /id="PRO_0000286514"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         271..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  38285 MW;  13392C6CE9204871 CRC64;
     MAAPLKVCIV GSGNWGSAIA RIIGSNAQKL QCFATTVKMW VYEEMVNGKK LSEIINTEHE
     NVKYLPGYKL PENVVAVPQL RDAADGADLL VFVVPHQFIR KLCDEMMGCV SERARGITLI
     KGIDEGPEGL KLISDIIREK MGIDVSVLMG ANIANEVAAE KFCESTIGSK VLENGLLFKD
     LLQTPNFRIT VVDDADTVEL CGALKNIVAV GAGFCDGLQC GDNTKAAVIR LGLMEMIAFA
     KLFSKDDSVS SATFLESCGV ADLITTCYGG RNRRVAEAFA KTGKSIEELE KEMLNGQKLQ
     GPLTSAEVYH ILKQKGLVEK FPLFTAVYQI CFEDKPVRDM ITCLQSHPEH L