GLPO_MYCGE
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 03-AUG-2022, entry version 91.
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; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
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 EnsemblBacteria; AAC71255; AAC71255; MG_039.
DR KEGG; mge:MG_039; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_3_0_14; -.
DR OMA; GVHFTRM; -.
DR OrthoDB; 1371190at2; -.
DR BioCyc; MGEN243273:G1GJ2-39-MON; -.
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; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 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
