ID Q833L7_ENTFA Unreviewed; 609 AA.
AC Q833L7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 08-NOV-2023, entry version 119.
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 OrderedLocusNames=EF_1928 {ECO:0000313|EMBL:AAO81679.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO81679.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO81679.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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}.
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DR EMBL; AE016830; AAO81679.1; -; Genomic_DNA.
DR RefSeq; NP_815609.1; NC_004668.1.
DR RefSeq; WP_002379559.1; NZ_KE136528.1.
DR AlphaFoldDB; Q833L7; -.
DR STRING; 226185.EF_1928; -.
DR EnsemblBacteria; AAO81679; AAO81679; EF_1928.
DR KEGG; efa:EF1928; -.
DR PATRIC; fig|226185.45.peg.1591; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_2_9; -.
DR OMA; WAMAPHI; -.
DR BRENDA; 1.1.3.21; 2095.
DR Proteomes; UP000001415; 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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001415}.
FT DOMAIN 21..352
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 609 AA; 67649 MW; 95FC886ABE220321 CRC64;
MTFSIETRRQ SIDALKTQHL DVLIIGGGIT GAGVALQASA AKMKTGLIEM QDFAEGTSSR
STKLVHGGIR YLKTFDVEVV ADTVKERAVV QSIAPHIPKA DPMLLPIYDE PNATFNLFSV
KIAMDLYDQL ADVTGTKYAN YLLTKDEVLA REPQLKSEGL QGGGVYLDYR NNDARLVIEN
IKQAVADGAH AVSRVQAVGF LYNDEGKITG IQAKDLLTDE QFEIHADVVI NTTGPWSDKL
RGLDKNDSFT PQMRPTKGVH LVVDKSRLNV PQPTYFDTGK QDGRMVFVVP REEKTYFGTT
DTDYHGDFQH PTVEQSDVDY LLEVVNNRYP EVQLTIDDIE ASWAGLRPLI SANGGSDYNG
GNNGKLSDKS IDEVIDVVDR YQKNQTDKRE IEEVLNHLED SLVENKVNPS AVSRGSSLER
SADGLLTLAG GKLTDYRKMA EGAMKMIQTI LAEEYQKEFT LIDSKNYPVS GGKLNPATVD
EELEALAKHG VSKGLSEKDA LYLAHLYGSN VPTVFEMIDD AKVIPGLTLT ETVSLNYAME
EEMALTPVDF LLRRTNHLLF MRDRLDQVKA GVIEEMAQHY QWTAEERARH IETLEKVIEE
SDLKNLKVG
//