GenomeNet

Database: UniProt
Entry: A0A0R2B0V4_9LACO
LinkDB: A0A0R2B0V4_9LACO
Original site: A0A0R2B0V4_9LACO 
ID   A0A0R2B0V4_9LACO        Unreviewed;       608 AA.
AC   A0A0R2B0V4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=FC34_GL001259 {ECO:0000313|EMBL:KRM71604.1};
OS   Lacticaseibacillus brantae DSM 23927.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1423727 {ECO:0000313|EMBL:KRM71604.1, ECO:0000313|Proteomes:UP000051672};
RN   [1] {ECO:0000313|EMBL:KRM71604.1, ECO:0000313|Proteomes:UP000051672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23927 {ECO:0000313|EMBL:KRM71604.1,
RC   ECO:0000313|Proteomes:UP000051672};
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:KRM71604.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AYZQ01000003; KRM71604.1; -; Genomic_DNA.
DR   RefSeq; WP_057894556.1; NZ_AYZQ01000003.1.
DR   AlphaFoldDB; A0A0R2B0V4; -.
DR   STRING; 1423727.FC34_GL001259; -.
DR   PATRIC; fig|1423727.3.peg.1280; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000051672; 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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051672}.
FT   DOMAIN          21..353
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          467..588
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   608 AA;  66028 MW;  28DA6CB8514C01EA CRC64;
     MAFSQKSRQQ TIENLKNTPL DLLIVGGGIT GAGVAIQAAA SGIKTGLIEM QDFAEGTSSR
     STKLVHGGIR YLKTFDVGVV SDTVKERAVV QGIAPHIPRP FPMLMPIYDE PDSTYDMFSV
     KIAMDLYDRL AGVTGTQYAN YTISKEEVLQ REPGLKPDKL LGGGVYLDFV NNDARLVIEN
     IKEADELGAN IASHVEATGV LYDDNGKVNG LKAHDNLTGE DFDIHAKLVI NTTGPWVDKF
     KSLDSKESQA PTLRPTKGVH LVVDDSRLSV PQPTYFDSGA DDGRMIFVVP REGKTYFGTT
     DTDFNGDYKH PTVEQSDVDY LLAAINNRYP EAGIKLDDVE ASWVGLRPLI AANGSSDYNG
     GGANAGKVSD ATFNALIDTV NDYEAKKADR AAVEKAISNL KTAHAEETLS PSQVSRGSSL
     KRADDGMITL SGGKITDYRK MAAGALALIR DILKSEYNVN AKEIDSTKLQ VSGGHFDPTN
     VDETIKFFAR IAQDAGLPEA DANDLANRFG SNTGRVVTYV QDGAAPGLSL KETISLRYSV
     NEEMALNPVD YLLRRTNAIL FHADTLNDLK EPVINEMARL LDWSDSEKAD QTEHLNQVIA
     ETQLDALK
//
DBGET integrated database retrieval system