ID   GPD2_CYBJA              Reviewed;         394 AA.
AC   Q6ZYA7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   13-SEP-2023, entry version 73.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2;
DE            EC=1.1.1.8;
GN   Name=gpd2;
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; AJ635370; CAG25779.2; -; Genomic_DNA.
DR   EMBL; AJ632340; CAG15348.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q6ZYA7; -.
DR   SMR; Q6ZYA7; -.
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..394
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 2"
FT                   /id="PRO_0000138094"
FT   ACT_SITE        243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         308..309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  43530 MW;  5970F34B5D528C15 CRC64;
     MTDIGESESD ISTDVSALPM LSHSVSYTSI QKPPFVVSVI GSGNWGTTVA KIIAENTREN
     PLLFEQKVRM WVYEEEFEGS NLSDIINTEH VNKKYLPGIK LPDNLVAVPD LLEAVQYSNI
     LIFNIPHQHL EKILSQLRGN IDPRARAISC LKGLRVNLDG VELLPDIIQD ALGIHCGVLA
     GANLAQEVAE QRFSETTVGY PLPADYKPGD VDHTVLYTLF HRPYFHVHVI EDIAGISCAG
     ALKNIIAISV GFVEGLEWGD NAKAAMLRRG LLEMIKFGRK FFPGCLVSSF TEESAGVADL
     FTTCTGGRNF KLAKIMAQTG KSAHEVEKEI LNGQSAQGLI TAKEIHELIK NKGCEEEFPL
     FETTYQILFH GVRIGILPYM LENKWSISKP NYSS
//