ID   GLPD_STAAC              Reviewed;         557 AA.
AC   Q5HGD1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=SACOL1321;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW38150.1; -; Genomic_DNA.
DR   RefSeq; WP_001218596.1; NC_002951.2.
DR   AlphaFoldDB; Q5HGD1; -.
DR   SMR; Q5HGD1; -.
DR   KEGG; sac:SACOL1321; -.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase.
FT   CHAIN           1..557
FT                   /note="Aerobic glycerol-3-phosphate dehydrogenase"
FT                   /id="PRO_0000270059"
FT   BINDING         21..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
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
//