ID   GLPD_STAEQ              Reviewed;         557 AA.
AC   Q5HPP0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=SERP0868;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
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; CP000029; AAW54267.1; -; Genomic_DNA.
DR   RefSeq; WP_002439581.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPP0; -.
DR   SMR; Q5HPP0; -.
DR   STRING; 176279.SERP0868; -.
DR   KEGG; ser:SERP0868; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000000531; 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;
KW   Reference proteome.
FT   CHAIN           1..557
FT                   /note="Aerobic glycerol-3-phosphate dehydrogenase"
FT                   /id="PRO_0000270065"
FT   BINDING         21..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   557 AA;  62276 MW;  6F6044C656324F7C CRC64;
     MSLSTLKRDH IKKNLRDTEY DVVIVGGGIT GAGIALDASN RGMKVALVEM QDFAQGTSSR
     STKLVHGGLR YLKQLQVGVV AETGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFSTSI
     GLAMYDRLAG VKKSERKKML SKQETLNKEP LVKRDGLKGG GYYVEYRTDD ARLTIEVMKK
     AAENGAEILN YTKSEHFTYD SNKKVNGIEV LDMIDGETYA IKAKKVINAS GPWVDEVRSG
     DYARNNKQLR LTKGVHVVID QSKFPLGQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD
     NEKATPLTTQ EDRDYLINAI NYMFPTVNVK DEDIESTWAG IRPLILEKGK DPSEISRKDE
     VWEGESGLLT IAGGKLTGYR HMALEIVDLL AKRLKQEYGL KFESCATKNL KISGGDVGGS
     KNFEHFVEQK VDAAKGFGID EDVARRLASK YGSNVDQLFN IAQTAPYHDS KLPLEIYVEL
     VYSIQQEMVY KPTDFLVRRS GKLYFNIQDV LDYKNAVIDV MADMLNYSET QKEAYTEEVE
     VAIDEARTGN DQPATKA
//