ID GLPO_STRP3 Reviewed; 612 AA.
AC P0DB20; Q8K666;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Alpha-glycerophosphate oxidase;
DE EC=1.1.3.21;
DE AltName: Full=Glycerol-3-phosphate oxidase;
GN Name=glpO; OrderedLocusNames=SpyM3_1467;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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; AE014074; AAM80074.1; -; Genomic_DNA.
DR RefSeq; WP_011054908.1; NC_004070.1.
DR AlphaFoldDB; P0DB20; -.
DR SMR; P0DB20; -.
DR KEGG; spg:SpyM3_1467; -.
DR HOGENOM; CLU_015740_5_2_9; -.
DR Proteomes; UP000000564; 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; 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 NCBIfam; NF033461; glycerol3P_ox_1; 1.
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.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase.
FT CHAIN 1..612
FT /note="Alpha-glycerophosphate oxidase"
FT /id="PRO_0000126111"
FT REGION 398..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; 67653 MW; 10BD47B2ED358B47 CRC64;
MEFSRETRRL ALQKMQERDL DLLIIGGGIT GAGVALQAAA SGLDTGLIEM QDFAQGTSSR
STKLVHGGLR YLKQFDVEVV SDTVSERAVV QQIAPHIPKP DPMLLPVYDE PGSTFSMFRL
KVAMDLYDLL AGVSNTPAAN KVLTKEEVLK REPDLKQEGL LGGGVYLDFR NNDARLVIEN
IKRANRDGAL IASHVKAEDF LLDDDGKIIG VKARDLLSDQ EIIIKAKLVI NTTGPWSDEI
RQFSHKGQPI HQMRPTKGVH LVVDRQKLPV SQPVYVDTGL NDGRMVFVLP REEKTYFGTT
DTDYTGDLEH PQVTQEDVDY LLGVVNNRFP NANVTIDDIE SSWAGLRPLL SGNSASDYNG
GNSGKVSDDS FDHLVDTVKA YINHEDSREA VEKAIKQVET STSEKELDPS AVSRGSSFDR
DENGLFTLAG GKITDYRKMA EGALTGIIQI LKEEFGKSFK LINSKTYPVS GGEINPANVD
LEIEAYAQLG TLSGLSMDDA RYLANLYGSN APKVFALTRQ LTAAEGLSLA ETLSLHYAMD
YEMALKPTDY FLRRTNHLLF MRDSLDALID PVINEMAKHF EWSDQERVAQ EDDLRRVIAD
NDLSALKGHQ EG
//
