ID   GLPD_STAS1              Reviewed;         557 AA.
AC   Q49X94;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=SSP1459;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008934; BAE18604.1; -; Genomic_DNA.
DR   RefSeq; WP_011303227.1; NZ_MTGA01000034.1.
DR   AlphaFoldDB; Q49X94; -.
DR   SMR; Q49X94; -.
DR   KEGG; ssp:SSP1459; -.
DR   PATRIC; fig|342451.11.peg.1463; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   OrthoDB; 9766796at2; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000006371; 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_0000270068"
FT   BINDING         21..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   557 AA;  62260 MW;  519E5CAF87EC8989 CRC64;
     MSLSTLKREQ IKKDLKDQEF DVVIIGGGIT GAGIALDASE RGMKVALVEM QDFAQGTSSR
     STKLVHGGLR YLKQLQVGVV AETGRERAIV YENGPHVTTP ERMLLPMHKG GSMGKFTTSI
     GLAMYDRLAG VKKAERKTML NAKETLEKEP LVKKAGLKGG GSYVEYRTDD ARLTIEVMKR
     AEEKGAKVIN HTKSVHFTYD SNEKVNGIQV EDQISNETYP IKAKKVINAS GPWVDEVRSG
     DYARNNKQLR LTKGVHIVID QSKFPLGQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD
     NNKTSPLANQ EDRDYLIDAI NYMFPDVNVA DEDIESSWAG VRPLILEEGK DPSEISRKDE
     VWEGKSGLLT IAGGKLTGYR HMALEIVDLL SKRLKSEFGL KFDKCATKHL TISGGDVGGS
     ANFDKFIEQK VEEAKSYQID ESTARHFASK YGSNAEELFK IAQTAQYQET GLPLDIYTEL
     VYSIQNEMVY RPTDFFIRRT GKLYFKIDDV LNYKEQVIDV MAGLLGYTNI EKEAYTKELQ
     IAIDEAQTGN HQPAVKE
//