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Database: UniProt
Entry: O14400
LinkDB: O14400
Original site: O14400 
ID   GPDM_SCHPO              Reviewed;         649 AA.
AC   O14400;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JAN-2019, entry version 136.
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; ORFNames=SPCC1223.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hansen K.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; Evidence={ECO:0000250};
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; Y14993; CAA75227.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA20872.1; -; Genomic_DNA.
DR   PIR; T40863; T40863.
DR   RefSeq; NP_588348.1; NM_001023339.2.
DR   ProteinModelPortal; O14400; -.
DR   SMR; O14400; -.
DR   BioGrid; 275787; 12.
DR   STRING; 4896.SPCC1223.03c.1; -.
DR   MaxQB; O14400; -.
DR   PaxDb; O14400; -.
DR   PRIDE; O14400; -.
DR   EnsemblFungi; SPCC1223.03c.1; SPCC1223.03c.1:pep; SPCC1223.03c.
DR   GeneID; 2539217; -.
DR   KEGG; spo:SPCC1223.03c; -.
DR   EuPathDB; FungiDB:SPCC1223.03c; -.
DR   PomBase; SPCC1223.03c; gut2.
DR   HOGENOM; HOG000004813; -.
DR   InParanoid; O14400; -.
DR   KO; K00111; -.
DR   OMA; MDNPTVK; -.
DR   PhylomeDB; O14400; -.
DR   Reactome; R-SPO-1483166; Synthesis of PA.
DR   Reactome; R-SPO-163560; Triglyceride catabolism.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:O14400; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
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:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISS:PomBase.
DR   GO; GO:0006116; P:NADH oxidation; ISO:PomBase.
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   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    649       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000010433.
FT   NP_BIND      69     97       FAD. {ECO:0000255}.
SQ   SEQUENCE   649 AA;  71873 MW;  65702D1FDE831E6A CRC64;
     MFSIFKRRSV QAALAASGLV GGAVFYSDFI KRPAPSHFNP QFTPFTKSLA PPPSRETLLK
     NVEDISKFDV LIIGGGATGT GVAVDASTRG LNVCLLEKTD FASETSSKST KMAHGGVRYL
     EKAVFQLSKA QLDLVIEALN ERANMLRTAP HLCTVLPIMI PVYKWWQVPY FFVGCKIYDW
     VAGSKNLRAS TIFSKETTVA IAPMLDDSNL KASCVYHDGS FNDTRMNTTL AVTAIDNGAT
     VLNYMEVKKL LKSKDNKLEG VLAIDRETGK EYQIKATSVV NATGPFSDKI LEMDADPQGE
     PPKTAQFPRM VVPSAGVHVV LPEYYCPPNI GILDPSTSDN RVMFFLPWQG KVIAGTTDKP
     LSSVPTNPTP SEDDIQLILK ELQKYLVFPV DREDVLSAWC GIRPLVRDPS TVPPGTDPTT
     GETQGLVRSH FIFKSDTGLL TISGGKWTTY REMAEETVNE LIKDHDFGKA LKPCQTKKLI
     LVGGENYYKN YSARLIHEYH IPLRLAKHLS HNYGSRAPLI LELYSKTDFN KLPVTLADKE
     VFAPSSDASS DKSVSYASFD EPFTVAELKY SIKYEYTRTP TDFLARRTRL AFLDARQALQ
     AVAGVTHVMK EEFGWDDATT DKLAQEARDY IGGMGVSSDR FDVKQFEVK
//
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