(data stored in ACNUC6288 zone)

SWISSPROT: Q6BM03_DEBHA

ID   Q6BM03_DEBHA            Unreviewed;       389 AA.
AC   Q6BM03;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 108.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE            EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN   OrderedLocusNames=DEHA2F09372g {ECO:0000313|EMBL:CAG89109.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89109.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89109.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8;
CC         Evidence={ECO:0000256|RuleBase:RU361243};
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU000437}.
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DR   EMBL; CR382138; CAG89109.1; -; Genomic_DNA.
DR   RefSeq; XP_460768.1; XM_460768.1.
DR   STRING; 4959.XP_460768.1; -.
DR   EnsemblFungi; CAG89109; CAG89109; DEHA2F09372g.
DR   GeneID; 2903610; -.
DR   KEGG; dha:DEHA2F09372g; -.
DR   HOGENOM; HOG000246855; -.
DR   InParanoid; Q6BM03; -.
DR   KO; K00006; -.
DR   OMA; WLCKGFE; -.
DR   OrthoDB; 476066at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM03.
DR   SWISS-2DPAGE; Q6BM03.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000437};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN       35    200       NAD_Gly3P_dh_N. {ECO:0000259|Pfam:
FT                                PF01210}.
FT   DOMAIN      233    378       NAD_Gly3P_dh_C. {ECO:0000259|Pfam:
FT                                PF07479}.
FT   NP_BIND      40     45       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   REGION      309    310       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   ACT_SITE    244    244       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000114-1}.
FT   BINDING      72     72       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     128    128       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     151    151       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   BINDING     184    184       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     309    309       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     338    338       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
SQ   SEQUENCE   389 AA;  42389 MW;  D77880495EF56DB6 CRC64;
     MSQYRANQRL QQLSNILRPN QLSAEKSLKP ETPFKVAVIG SGNWGTTIAK VLAENTAEKP
     DTFAKQVDMW VFQEKIDGTN LTEIINNKHE NVKYLPGVKL PENLHAEPDI VKAAQGADLL
     VFNLPHQFLP KICKQLKGTL KPTTRAISCL KGLEVTPDGC KLLSTYITEN LGIECGALSG
     ANLAPEVARC KWSETTVAYN IPADFKGPGK DIDSAVLKEA FHRPYFHVNV IEDVAGVSVA
     GALKNIVAIA VGFVEGLGWG DNAKSAIMRV GLIETINFSN MFFPNSKPTT FTHESAGVAD
     LITTCSGGRN VKVGRHMSKT GESAEEAEKK LLNGQSSQGI ITAKEVHELL SNVGKTDQFP
     LFEATYQIIY GDESIQNLPN LLEDHSLFK
//

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