GPDM_YEAST
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 03-AUG-2022, entry version 181.
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; 79.
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; YIL155C.
DR GeneID; 854651; -.
DR KEGG; sce:YIL155C; -.
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; CIVNAAG; -.
DR BioCyc; MetaCyc:YIL155C-MON; -.
DR BioCyc; YEAST:YIL155C-MON; -.
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 RNAct; P32191; protein.
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: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:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IDA: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 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
