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Database: UniProt
Entry: P32191
LinkDB: P32191
Original site: P32191 
ID   GPDM_YEAST              Reviewed;         649 AA.
AC   P32191; D6VVD2; E9P8Y2;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   13-FEB-2019, entry version 164.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3;
DE   Flags: Precursor;
GN   Name=GUT2; OrderedLocusNames=YIL155C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=8256521; DOI=10.1002/yea.320091013;
RA   Roennow B., Kielland-Brandt M.C.;
RT   "GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of
RT   Saccharomyces cerevisiae.";
RL   Yeast 9:1121-1130(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
RA   Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
RA   Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
RA   Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11502169; DOI=10.1021/bi010277r;
RA   Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
RA   Manon S., Schmitter J.-M.;
RT   "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT   complex.";
RL   Biochemistry 40:9758-9769(2001).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=22984289; DOI=10.1074/mcp.M112.021105;
RA   Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA   Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT   "Intermembrane space proteome of yeast mitochondria.";
RL   Mol. Cell. Proteomics 11:1840-1852(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:11502169}. Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:22984289}.
CC   -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; Z38059; CAA86123.1; -; Genomic_DNA.
DR   EMBL; X71660; CAA50652.1; -; Genomic_DNA.
DR   EMBL; AY692867; AAT92886.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08398.1; -; Genomic_DNA.
DR   PIR; S38190; S48379.
DR   RefSeq; NP_012111.1; NM_001179503.1.
DR   ProteinModelPortal; P32191; -.
DR   BioGrid; 34837; 73.
DR   DIP; DIP-7385N; -.
DR   IntAct; P32191; 3.
DR   STRING; 4932.YIL155C; -.
DR   iPTMnet; P32191; -.
DR   MaxQB; P32191; -.
DR   PaxDb; P32191; -.
DR   PRIDE; P32191; -.
DR   EnsemblFungi; YIL155C_mRNA; YIL155C_mRNA; YIL155C.
DR   GeneID; 854651; -.
DR   KEGG; sce:YIL155C; -.
DR   EuPathDB; FungiDB:YIL155C; -.
DR   SGD; S000001417; GUT2.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOGENOM; HOG000004813; -.
DR   InParanoid; P32191; -.
DR   KO; K00111; -.
DR   OMA; MDNPTVK; -.
DR   BioCyc; YEAST:YIL155C-MONOMER; -.
DR   Reactome; R-SCE-1483166; Synthesis of PA.
DR   Reactome; R-SCE-163560; Triglyceride catabolism.
DR   SABIO-RK; P32191; -.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:P32191; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:SGD.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IMP:SGD.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR   GO; GO:0001302; P:replicative cell aging; IMP:SGD.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    649       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000010434.
FT   NP_BIND      69     97       FAD. {ECO:0000255}.
FT   CONFLICT      1     51       MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSY
FT                                MVQFPTAAPP -> MTRATWCNSPPPLHR (in Ref.
FT                                1). {ECO:0000305}.
FT   CONFLICT     63     63       A -> D (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
FT   CONFLICT    182    182       A -> G (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
FT   CONFLICT    234    234       A -> G (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
FT   CONFLICT    243    243       N -> I (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
FT   CONFLICT    249    249       K -> R (in Ref. 4; AAT92886).
FT                                {ECO:0000305}.
FT   CONFLICT    320    320       A -> S (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
FT   CONFLICT    342    342       C -> S (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
FT   CONFLICT    645    646       KT -> QGR (in Ref. 1; CAA50652).
FT                                {ECO:0000305}.
SQ   SEQUENCE   649 AA;  72389 MW;  FE6B25F5B21EF8DA CRC64;
     MFSVTRRRAA GAAAAMATAT GTLYWMTSQG DRPLVHNDPS YMVQFPTAAP PQVSRRDLLD
     RLAKTHQFDV LIIGGGATGT GCALDAATRG LNVALVEKGD FASGTSSKST KMIHGGVRYL
     EKAFWEFSKA QLDLVIEALN ERKHLINTAP HLCTVLPILI PIYSTWQVPY IYMGCKFYDF
     FAGSQNLKKS YLLSKSATVE KAPMLTTDNL KASLVYHDGS FNDSRLNATL AITAVENGAT
     VLNYVEVQKL IKDPTSGKVI GAEARDVETN ELVRINAKCV VNATGPYSDA ILQMDRNPSG
     LPDSPLNDNS KIKSTFNQIA VMDPKMVIPS IGVHIVLPSF YCPKDMGLLD VRTSDGRVMF
     FLPWQGKVLA GTTDIPLKQV PENPMPTEAD IQDILKELQH YIEFPVKRED VLSAWAGVRP
     LVRDPRTIPA DGKKGSATQG VVRSHFLFTS DNGLITIAGG KWTTYRQMAE ETVDKVVEVG
     GFHNLKPCHT RDIKLAGAEE WTQNYVALLA QNYHLSSKMS NYLVQNYGTR SSIICEFFKE
     SMENKLPLSL ADKENNVIYS SEENNLVNFD TFRYPFTIGE LKYSMQYEYC RTPLDFLLRR
     TRFAFLDAKE ALNAVHATVK VMGDEFNWSE KKRQWELEKT VNFIKTFGV
//
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