ID   GLPD_PSEAE              Reviewed;         512 AA.
AC   P52111;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=PA3584;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CD10;
RX   PubMed=8157588; DOI=10.1128/jb.176.8.2184-2193.1994;
RA   Schweizer H.P., Po C.;
RT   "Cloning and nucleotide sequence of the glpD gene encoding sn-glycerol-3-
RT   phosphate dehydrogenase of Pseudomonas aeruginosa.";
RL   J. Bacteriol. 176:2184-2193(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; L06231; AAA81584.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06972.1; -; Genomic_DNA.
DR   PIR; A55207; A55207.
DR   PIR; B83197; B83197.
DR   RefSeq; NP_252274.1; NC_002516.2.
DR   RefSeq; WP_003098460.1; NZ_QZGE01000001.1.
DR   AlphaFoldDB; P52111; -.
DR   SMR; P52111; -.
DR   STRING; 208964.PA3584; -.
DR   PaxDb; 208964-PA3584; -.
DR   GeneID; 880179; -.
DR   KEGG; pae:PA3584; -.
DR   PATRIC; fig|208964.12.peg.3751; -.
DR   PseudoCAP; PA3584; -.
DR   HOGENOM; CLU_015740_5_0_6; -.
DR   InParanoid; P52111; -.
DR   OrthoDB; 9766796at2; -.
DR   PhylomeDB; P52111; -.
DR   BioCyc; PAER208964:G1FZ6-3653-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR   Gene3D; 6.10.250.1890; -; 1.
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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
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..512
FT                   /note="Glycerol-3-phosphate dehydrogenase"
FT                   /id="PRO_0000126104"
FT   BINDING         16..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        77..78
FT                   /note="EA -> DT (in Ref. 1; AAA81584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133..140
FT                   /note="GLRFTGSS -> ACVHRQQ (in Ref. 1; AAA81584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180..208
FT                   /note="RTRCVSARRSKGLWHLHLERSDGSLYSIR -> APAASAPVAARDSGTCTWS
FT                   AATAACIRS (in Ref. 1; AAA81584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425..430
FT                   /note="LRWART -> PALGAH (in Ref. 1; AAA81584)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  57135 MW;  DFF734821ABD730C CRC64;
     MSQAHTPSAP LAEVYDVAVV GGGINGVGIA ADAAGRGLSV FLCEQHDLAQ HTSSASSKLI
     HGGLRYLEHY EFRLVREALA EREVLLAKAP HIVKPLRFVL PHRPHLRPAW MIRAGLFLYD
     HLGKREKLPA SRGLRFTGSS PLKAEIRRGF EYSDCAVDDA RLVVLNAISA REHGAHVHTR
     TRCVSARRSK GLWHLHLERS DGSLYSIRAR ALVNAAGPWV ARFIQDDLKQ KSPYGIRLIQ
     GSHIIVPKLY EGEHAYILQN EDRRIVFAIP YLDRFTMIGT TDREYQGDPA KVAISEEETA
     YLLQVVNAHF KQQLAAADIL HSFAGVRPLC DDESDEPSAI TRDYTLSLSA GNGEPPLLSV
     FGGKLTTYRK LAESALTQLQ PFFANLGPAW TAKAPLPGGE QMQSVEALTE QLANRYAWLD
     RELALRWART YGTRVWRLLD GVNGEADLGE HLGGGLYARE VDYLCKHEWA QDAEDILWRR
     SKLGLFLSPS QQVRLGQYLQ SEHPHRPRVH AA
//