ID   GLPO_MYCGE              Reviewed;         384 AA.
AC   P47285;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Glycerol 3-phosphate oxidase {ECO:0000250|UniProtKB:P75063};
DE            Short=GlpO;
DE            EC=1.1.3.21 {ECO:0000250|UniProtKB:P75063};
DE   AltName: Full=L-alpha-glycerophosphate oxidase;
DE   Flags: Precursor;
GN   OrderedLocusNames=MG039;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
CC   -!- FUNCTION: Catalyzes the oxidation of glycerol 3-phosphate to
CC       dihydroxyacetone phosphate (DHAP), with a reduction of O2 to H2O2. The
CC       formation of hydrogen peroxide by this enzyme is crucial for cytotoxic
CC       effects on host cells. Does not show any dehydrogenase activity with
CC       NAD(+). {ECO:0000250|UniProtKB:P75063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate +
CC         H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642; EC=1.1.3.21;
CC         Evidence={ECO:0000250|UniProtKB:P75063};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18370;
CC         Evidence={ECO:0000250|UniProtKB:P75063};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P75063};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1. {ECO:0000250|UniProtKB:P75063}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P75063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P75063}. Cell
CC       membrane {ECO:0000250|UniProtKB:P75063, ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR   EMBL; L43967; AAC71255.1; -; Genomic_DNA.
DR   PIR; C64204; C64204.
DR   RefSeq; WP_010869301.1; NC_000908.2.
DR   AlphaFoldDB; P47285; -.
DR   SMR; P47285; -.
DR   STRING; 243273.MG_039; -.
DR   KEGG; mge:MG_039; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_024775_3_0_14; -.
DR   InParanoid; P47285; -.
DR   OrthoDB; 9801699at2; -.
DR   BioCyc; MGEN243273:G1GJ2-39-MONOMER; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
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; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   NCBIfam; NF033460; glycerol3P_ox_II; 1.
DR   PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1.
DR   PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism;
KW   Lipoprotein; Membrane; Oxidoreductase; Palmitate; Reference proteome;
KW   Signal; Virulence.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..384
FT                   /note="Glycerol 3-phosphate oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000210395"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         42..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         47..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         47
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         51
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         177
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         258
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         320
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         346..347
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         348
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   BINDING         352
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P75063"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   384 AA;  42796 MW;  3273E860B5EE94A8 CRC64;
     MQTIDVLIVG GGVIGTSCAY ELSQYKLKVA LLEKNAFLGC ETSQANSGVI HSGIDPNPNK
     LTAKYNILGR KIWIEDWFKK LIFPRKKIAT LIVAFNNEEK LQLNLLKERG IKNSIPVENI
     QILDQQQTLL QEPFINPNVV ASLKVEGSWL IDPLIATKCL ALASLQNNVA IYSNKKVTKI
     EIDSDDDFLV FINNETTPQF KTKKLIDAAG HYADWLAETT QVDNFKQTTR KGQYLVLKNQ
     NNLKINTIIF MVPTIHGKGV VVAEMLDGNI LVGPNAVEGI EKNKTRSIDL DSINQIKTIG
     KKMVPSLQFE NSIYSFAGSR AIDIETNDFV IRTAKSNPNF IILGGMKSPG LTSSPAIAKR
     AVELLNLKLK KKINWNPNYN LSWI
//