GLPO_STRP6
ID GLPO_STRP6 Reviewed; 612 AA.
AC Q5XAK0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-glycerophosphate oxidase;
DE EC=1.1.3.21;
DE AltName: Full=Glycerol-3-phosphate oxidase;
GN Name=glpO; Synonyms=glpA; OrderedLocusNames=M6_Spy1428;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- CAUTION: As S.pyogenes is unable to produce acid from glycerol, the
CC significance and/or function of the glpO gene in this organism is at
CC present unknown. {ECO:0000305}.
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DR EMBL; CP000003; AAT87563.1; -; Genomic_DNA.
DR RefSeq; WP_011184846.1; NC_006086.1.
DR AlphaFoldDB; Q5XAK0; -.
DR SMR; Q5XAK0; -.
DR EnsemblBacteria; AAT87563; AAT87563; M6_Spy1428.
DR KEGG; spa:M6_Spy1428; -.
DR HOGENOM; CLU_015740_5_2_9; -.
DR OMA; CIVNAAG; -.
DR Proteomes; UP000001167; 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:InterPro.
DR GO; GO:0004369; F:glycerol-3-phosphate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
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; PTHR11985; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase.
FT CHAIN 1..612
FT /note="Alpha-glycerophosphate oxidase"
FT /id="PRO_0000126112"
FT REGION 399..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 612 AA; 67914 MW; 341CDF7964357A57 CRC64;
MEFSKETRRL ALQKMQERDL DLLIIGGGIT GAGVALQAAA SGLDTGLIEM QDFAEGTSSR
STKLVHGGLR YLKQFDVEVV SDTVSERAVV QQIAPHIPKP DPMLLPVYDE PGSTFSMFRL
KVAMDLYDLL AGVSNTPAAN KVLTKEEVLK REPDLKQEGL LGGGVYLDFR NNDARLVIEN
IKRANRDGAL IASHVKAEDF LLDDKRQIIG VKARDLLTDQ EIIIKAKLVI NTTGPWSDEI
RQFSHKGQPI HQMRPTKGVH LVVDRQKLPV SQPVYVDTGL NDGRMVFVLP REEKTYFGTT
DTDYTGDLQH PQVTQEDVDY LLGIVNNRFP NANLTINDIE SSWAGLRPLL SGNSASDYNG
GNSGKLSDDS FDHLIDTVKA YINHEDSREA VEKAIKQVET STSEKELDPS AVSRGSSFER
DENGLFTLAG GKITDYRKMA EGALKVIIQV LKEDFGKSFK LINSTTYPVS GGEINPANVD
SELEAYAQLG TLSGLSMDDA RYLANLYGSN APKVFALTRQ LKAAEGLSLA ETLSLHYAMD
YEMALKPTDY FLRRTNHLLF MRDSLDALIV PVIEEMAKHF DWSTDEKVKQ EEELRRVIAE
NDLSALKGQQ ED