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 27-MAR-2024, entry version 97.
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; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAG43012.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571857; CAG43012.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001218596.1; NC_002953.3.
DR AlphaFoldDB; Q6G9R2; -.
DR SMR; Q6G9R2; -.
DR KEGG; sas:SAS1234; -.
DR HOGENOM; CLU_015740_5_2_9; -.
DR UniPathway; UPA00618; UER00674.
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_0000270063"
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
//
