ID   GPD_LACTH               Reviewed;         411 AA.
AC   Q7ZA45;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)];
DE            EC=1.1.1.8;
GN   Name=GPD;
OS   Lachancea thermotolerans (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=381046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 137;
RX   PubMed=15381122; DOI=10.1016/j.femsyr.2004.06.012;
RA   Neves L., Oliveira R., Lucas C.;
RT   "Yeast orthologues associated with glycerol transport and metabolism.";
RL   FEMS Yeast Res. 5:51-62(2004).
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   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AY289713; AAP44104.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7ZA45; -.
DR   SMR; Q7ZA45; -.
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   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..411
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]"
FT                   /id="PRO_0000138090"
FT   ACT_SITE        275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         71..76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         103
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         215
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         340..341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         340
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         369
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
SQ   SEQUENCE   411 AA;  45332 MW;  A155FF3F16521A86 CRC64;
     MFSISRITRT SSFTTQFRAL YRFKHSARKL QSIPFSIYKK MSAADRLNQT HDILSESVQA
     VENPFKVTVI GSGNWGTTIS KVVAENAALR PHLFVKRVDM WVFEETVDGQ KLTEIINTKH
     QNVKYLPNID LPENLVANPD LVSAVKDADI LVFNIPHQFL PRIVSQLQGN IKKDARAISC
     LKGFDVSKDG VKLLSTYVTE KLGITCGALS GANLAPEVAK ENWSETTVAY ELPKDFKGEG
     KDVDHAVLKA LFHRPYFHVN VIDDVAGISV AGALKNVVAL GCGFVEGLGW GNNASAAIQR
     VGLGEIIKFG QMFFPDSRVE TYYQESAGVA DLITTCSGGR NVRVATHMAK TGKSAEECEK
     ELLNGQSAQV FTHVRRSTSG WPSAVRPMNS FCSRPFTRLS TRTLLWTLCQ T