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   27-MAR-2024, entry version 189.
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; Saccharomycetes;
OC   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., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   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., Manon S.,
RA   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., Dephoure N.,
RA   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 SCALE
RP   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, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, 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 kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       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 medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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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   AlphaFoldDB; P32191; -.
DR   SMR; P32191; -.
DR   BioGRID; 34837; 86.
DR   DIP; DIP-7385N; -.
DR   IntAct; P32191; 3.
DR   STRING; 4932.YIL155C; -.
DR   iPTMnet; P32191; -.
DR   MaxQB; P32191; -.
DR   PaxDb; 4932-YIL155C; -.
DR   PeptideAtlas; P32191; -.
DR   EnsemblFungi; YIL155C_mRNA; YIL155C; YIL155C.
DR   GeneID; 854651; -.
DR   KEGG; sce:YIL155C; -.
DR   AGR; SGD:S000001417; -.
DR   SGD; S000001417; GUT2.
DR   VEuPathDB; FungiDB:YIL155C; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOGENOM; CLU_015740_4_1_1; -.
DR   InParanoid; P32191; -.
DR   OMA; PHIVKPM; -.
DR   OrthoDB; 989271at2759; -.
DR   BioCyc; MetaCyc:YIL155C-MONOMER; -.
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   BioGRID-ORCS; 854651; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P32191; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P32191; Protein.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:SGD.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IMP:SGD.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..649
FT                   /note="Glycerol-3-phosphate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000010434"
FT   BINDING         69..97
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..51
FT                   /note="MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSYMVQFPTAAPP
FT                   -> MTRATWCNSPPPLHR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="A -> D (in Ref. 1; CAA50652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="A -> G (in Ref. 1; CAA50652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="A -> G (in Ref. 1; CAA50652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="N -> I (in Ref. 1; CAA50652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="K -> R (in Ref. 4; AAT92886)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="A -> S (in Ref. 1; CAA50652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="C -> S (in Ref. 1; CAA50652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        645..646
FT                   /note="KT -> QGR (in Ref. 1; CAA50652)"
FT                   /evidence="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
//