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Database: UniProt
Entry: Q833L7_ENTFA
LinkDB: Q833L7_ENTFA
Original site: Q833L7_ENTFA 
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
//
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