ID   GPD1_PICJA              Reviewed;         393 AA.
AC   Q6ZZF4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 27.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+] 1;
DE            EC=1.1.1.8;
GN   Name=gpd1;
OS   Pichia jadinii (Yeast) (Candida utilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9950 / CBS 5609 / DSM 2361 / IFO 0998 / NRRL Y-900;
RX   PubMed=17381046; DOI=10.1080/10425170600807165;
RA   Ostermann K., Richter M., Zscharnack M., Rothe R., Walther T.,
RA   Roedel G.;
RT   "Identification of the genes GPD1 and GPD2 of Pichia jadinii.";
RL   DNA Seq. 17:452-457(2006).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone
CC       phosphate + NADH.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; AJ632339; CAG15347.1; -; Genomic_DNA.
DR   EMBL; AJ632341; CAG15350.1; -; Genomic_DNA.
DR   HSSP; P90551; 1JDJ.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase (NAD+) a...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; 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   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013328; DHase_multihelical.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR017751; NAD-dep_Gly3P_DH_euk.
DR   InterPro; IPR006168; NAD-dep_Gly3P_DHase.
DR   InterPro; IPR011128; NAD-dep_Gly3P_DHase_N.
DR   InterPro; IPR006109; NAD_Gly3P_DHase_C.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   PANTHER; PTHR11728; NAD_Gly3P_DH; 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   ProDom; PD001278; NAD_Gly3P_C; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    393       Glycerol-3-phosphate dehydrogenase [NAD+]
FT                                1.
FT                                /FTId=PRO_0000138093.
FT   NP_BIND      45     50       NAD (By similarity).
FT   REGION      316    317       Substrate binding (By similarity).
FT   ACT_SITE    250    250       Proton acceptor (By similarity).
FT   BINDING     133    133       NAD (By similarity).
FT   BINDING     157    157       NAD; via amide nitrogen (By similarity).
FT   BINDING     157    157       Substrate (By similarity).
FT   BINDING     190    190       NAD; via amide nitrogen (By similarity).
FT   BINDING     316    316       NAD (By similarity).
FT   BINDING     345    345       NAD (By similarity).
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
//