ID A0A1E5GQ56_9ENTE Unreviewed; 611 AA.
AC A0A1E5GQ56;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Alpha-glycerophosphate oxidase {ECO:0000256|ARBA:ARBA00021658};
DE EC=1.1.3.21 {ECO:0000256|ARBA:ARBA00013104};
DE AltName: Full=Glycerol-3-phosphate oxidase {ECO:0000256|ARBA:ARBA00032349};
GN ORFNames=BCR23_11985 {ECO:0000313|EMBL:OEG14809.1};
OS Enterococcus quebecensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=903983 {ECO:0000313|EMBL:OEG14809.1, ECO:0000313|Proteomes:UP000094764};
RN [1] {ECO:0000313|EMBL:OEG14809.1, ECO:0000313|Proteomes:UP000094764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26306 {ECO:0000313|EMBL:OEG14809.1,
RC ECO:0000313|Proteomes:UP000094764};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000275};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEG14809.1}.
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DR EMBL; MIKB01000018; OEG14809.1; -; Genomic_DNA.
DR RefSeq; WP_069636040.1; NZ_MIKB01000018.1.
DR AlphaFoldDB; A0A1E5GQ56; -.
DR STRING; 903983.BCR23_11985; -.
DR PATRIC; fig|903983.4.peg.501; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000094764; Unassembled WGS sequence.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 21..351
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 465..587
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 611 AA; 67835 MW; 9C013F2B05B2A450 CRC64;
MTFSIKTRQE SIEKLKHGEL DLLIIGGGIT GAGVALQASA AGMKTGLIEM QDFAEGTSSR
STKLVHGGIR YLKNFDVEVV ADTVQERAVV QAIAPHIPKP DPMLLPIYDE PKATFNMFSV
KVAMDLYDRL ANVIGTKYEN YTLTKEEVLE REPQLKSEGL QGGGVYLDFR NNDARLVIEN
IKQASQDGGL MVSKVKAVGF IFNGEGKITG VKAKDLLTDE IFEINAKVII NTTGPWSDKV
RGLDTAKKLI PQMRPTKGVH LVVDSSKLFV PQPTYFDTGK HDGRMVFVVP REKKTYFGTT
DTDYTGDYEH PTVTQEDVDY LLEIVNNRYP QANVTIADIE ASWAGLRPLI SENGGSDYNG
GNNGKVSDKS FDQVIDIVSK YQKQEVSRYD VENVLNHLED SLAESKENPS AVSRGSLLER
SEDGLLTLSG GKITDYRKMA EGALKEIQRI LKEEFDRTFQ LIDSKTYPVS GGRINPANVE
TELETLAKNG IEKGLTKEEA EYLAHLYGSN VTKVFGKIDE TKPVAGLSLA ETIALHYALE
NEMALTPADY LVRRTNHILF MRDTLDEVKQ GVIAEMSNYY TWSDEQKEIY TNELNELIAE
SDLSLLKEGA K
//
