ID   GLPD_STAAS              Reviewed;         557 AA.
AC   Q6G9R2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=SAS1234;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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       (aerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX571857; CAG43012.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_043361.1; -.
DR   GeneID; 2863533; -.
DR   GenomeReviews; BX571857_GR; SAS1234.
DR   KEGG; sas:SAS1234; -.
DR   HOGENOM; Q6G9R2; -.
DR   BioCyc; SAUR282459:SAS1234-MON; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism;
KW   Oxidoreductase.
FT   CHAIN         1    557       Aerobic glycerol-3-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000270063.
FT   NP_BIND      21     49       FAD (Potential).
SQ   SEQUENCE   557 AA;  62388 MW;  BB3D044040212E82 CRC64;
     MALSTFKREH IKKNLRNDEY DLVIIGGGIT GAGIALDASE RGMKVALVEM QDFAQGTSSR
     STKLVHGGLR YLKQFQIGVV AETGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFSTSI
     GLGMYDRLAG VKKSERKKML SKKETLAKEP LVKKEGLKGG GYYVEYRTDD ARLTIEVMKR
     AAEKGAEIIN YTKSEHFTYD KNQQVNGVKV IDKLTNENYT IKAKKVVNAA GPWVDDVRSG
     DYARNNKKLR LTKGVHVVID QSKFPLGQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD
     NIKSSPLTTQ EDRDYLIDAI NYMFPSVNVT DEDIESTWAG IRPLIYEEGK DPSEISRKDE
     IWEGKSGLLT IAGGKLTGYR HMAQDIVDLV SKRLKKDYGL TFSPCNTKGL AISGGDVGGS
     KNFDAFVEQK VDVAKGFGID EDVARRLASK YGSNVDELFN IAQTSQYHDS KLPLEIYVEL
     VYSIQQEMVY KPNDFLVRRS GKMYFNIKDV LDYKDAVIDI MADMLDYSPA QIEAYTEEVE
     QAIKEAQHGN NQPAVKE
//