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-JUN-2009, entry version 65.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPDH-M;
DE            Short=GPD-M;
DE            EC=1.1.5.3;
DE   Flags: Precursor;
GN   Name=gut2; ORFNames=SPCC1223.03c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
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=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR: FAD (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; Y14993; CAA75227.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA20872.1; -; Genomic_DNA.
DR   PIR; T40863; T40863.
DR   RefSeq; NP_588348.1; -.
DR   GeneID; 2539217; -.
DR   KEGG; spo:SPCC1223.03c; -.
DR   NMPDR; fig|4896.1.peg.686; -.
DR   GeneDB_Spombe; SPCC1223.03c; -.
DR   OMA; O14400; RTRFAFL.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000268-MON; -.
DR   BRENDA; 1.1.99.5; 653.
DR   ArrayExpress; O14400; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:GeneDB_SPombe.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0033554; P:cellular response to stress; IEP:GeneDB_SPombe.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000447; FAD-dep_Gly3P_DH.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    649       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000010433.
FT   NP_BIND      69     97       FAD (Potential).
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
//