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Database: UniProt
Entry: A0A0R2FGF0_9LACO
LinkDB: A0A0R2FGF0_9LACO
Original site: A0A0R2FGF0_9LACO 
ID   A0A0R2FGF0_9LACO        Unreviewed;       581 AA.
AC   A0A0R2FGF0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=IV36_GL001792 {ECO:0000313|EMBL:KRN26635.1};
OS   Liquorilactobacillus mali.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1618 {ECO:0000313|EMBL:KRN26635.1, ECO:0000313|Proteomes:UP000051727};
RN   [1] {ECO:0000313|EMBL:KRN26635.1, ECO:0000313|Proteomes:UP000051727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27304 {ECO:0000313|EMBL:KRN26635.1,
RC   ECO:0000313|Proteomes:UP000051727};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN26635.1}.
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DR   EMBL; JQAR01000040; KRN26635.1; -; Genomic_DNA.
DR   RefSeq; WP_056992568.1; NZ_WERQ01000013.1.
DR   AlphaFoldDB; A0A0R2FGF0; -.
DR   STRING; 1618.IV36_GL001792; -.
DR   PATRIC; fig|1618.3.peg.1824; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000051727; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..358
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          432..553
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   581 AA;  63862 MW;  B7EFC829BE9B5838 CRC64;
     MSFSINSRKS DIQKLKREQQ DLLIIGGGIT GAGVALQASA AGMKTALIDM QDFGGGTSSR
     STRLVHGGIR YLKTFDVEVV SDTVKERAVV QHIAPHMVRP DPMLLPIYDE PGTTFTMFSV
     KVAMDLYDHL AGINKTPNLK KYANYMLTKE EVLKREPQLN PENLAGGGVY LDYQNNDSRL
     VVENIKKAHE KGGLMVSRLK AIKILNDGNG HVIGVKVKDT LTNEEFDIQA KVVINTSGPW
     SDFVRHLDED EDKKSQMRPT KGVHLVVDQS RLKVPQPTYF GSGTNDGRMI FTIPREGKTY
     FGTTDTDYKG DLTNPRVDMN DVDYLLKIIN KKYPHAHLTL ADVETSWAGV RPLVAAEEPE
     TDVVSGASDA GNASAPSAVS RGSSLKVAQD GLITLAGGKL TDYRVMADGA MKKIITILHD
     QFDENFEEVN SAELKVSGGD FDSDKAEEIL DSYAKQGVAK GFTPAEAEEI VTLFGSNSLK
     IFAAADKATA APGLSLAETL SLHYSLDEEM TLTPVDYLLR RTYHLLFRSE TLDKVKQGVI
     NEMARYFAWD QAEVAEQTEL LDKEIAAAKL VDLKHNRSVT N
//
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