ID   GLPD_STAHJ              Reviewed;         557 AA.
AC   Q4L608;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=SH1608;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE04917.1; -; Genomic_DNA.
DR   RefSeq; WP_011275898.1; NC_007168.1.
DR   AlphaFoldDB; Q4L608; -.
DR   SMR; Q4L608; -.
DR   GeneID; 58062197; -.
DR   KEGG; sha:SH1608; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   OrthoDB; 9766796at2; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000000543; 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_0000270067"
FT   BINDING         21..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   557 AA;  62821 MW;  0856390DC2F7AB13 CRC64;
     MALSTLNREV IKKNLQNEEY DVVIIGGGIT GAGIALDASQ RGMKVALVEM QDFAQGTSSR
     STKLVHGGLR YLKQAQIKVV AETGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFTTNL
     GLTAYDRLAG VKKYERKKML SKKQTLNKEP LVKKDGLKGG GYYVEYRTDD ARLTIEVMKR
     AEENGAEILN HTKSTDFIYD SKSKVRGIEV QDLLTGEMYE INAKKVINAA GPWVDEVRKK
     DYTRNNKQLR LTKGVHVVID QSKFPLRQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD
     NDKTKPLTTQ EDRDYLIDAI NYMFPDVNVK DEDIESTWAG VRPLILEDGK DPSEISRKDE
     IWEGKSGLLT IAGGKLTGYR HMALEIVDLL AKRLKQEYKL TFAECKTKHT PISGGDVGGS
     ANFESFVERK VEEGKAIGLQ ADVAKRLASK YGSNVDKLYN IAQIAQDKDL KLPLELYVEL
     VYSVQNEMVF KPTDFLIRRS GKLYFNINEV KQYKDAVVEE LAKLLNYTQS QQNEFTKEIN
     IAIEEATRGN EQLAVLK
//