ID   GPD1_CYBJA              Reviewed;         393 AA.
AC   Q6ZZF4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   13-SEP-2023, entry version 75.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1;
DE            EC=1.1.1.8;
GN   Name=gpd1;
OS   Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900;
RX   PubMed=17381046; DOI=10.1080/10425170600807165;
RA   Ostermann K., Richter M., Zscharnack M., Rothe R., Walther T., Roedel G.;
RT   "Identification of the genes GPD1 and GPD2 of Pichia jadinii.";
RL   DNA Seq. 17:452-457(2006).
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; AJ632339; CAG15347.1; -; Genomic_DNA.
DR   EMBL; AJ632341; CAG15350.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6ZZF4; -.
DR   SMR; Q6ZZF4; -.
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:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 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.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..393
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1"
FT                   /id="PRO_0000138093"
FT   ACT_SITE        250
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..50
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         316..317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  42957 MW;  A87107CBB8B605D9 CRC64;
     MLRIGKLNLS TMSSAQQRLA QVGSHLTAQK QSLAPQRPYK ITVIGSGNWG TTIAKVLAEN
     AGLRPHLFQH QVDMWVFEEK INGVNLTEII NTQHENVKYL PGIKLPKNLH AEPSIVKAAE
     GADLLVFNIP HQFLPGICKQ LSKATLKPHV RAISCLKGLE VTPNGCKLLS TYITEHLGVH
     CGALSGANLA PEVAKEKWSE TTVAYRLPND FQGHGKDIDR YVLRAAFHRP YFHVRVIEDV
     AGVSLAGALK NVVALGVGFV HGLNWGDNAA SAIQRFGLNE TIKFAEVFFP GETNQDTFTK
     ESAGVADLIT TCSGGRNVRV AKAMAITGKS AVEVERELLN GQSAQGIITS KEVHELLAAK
     NLTKEFPLFE AIYQIVYGTE SIERLPELIE EDE
//