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Database: UniProt
Entry: H3NBU6_9LACT
LinkDB: H3NBU6_9LACT
Original site: H3NBU6_9LACT 
ID   H3NBU6_9LACT            Unreviewed;       606 AA.
AC   H3NBU6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=HMPREF9703_00027 {ECO:0000313|EMBL:EHR35179.1};
OS   Dolosigranulum pigrum ATCC 51524.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Dolosigranulum.
OX   NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR35179.1, ECO:0000313|Proteomes:UP000003599};
RN   [1] {ECO:0000313|EMBL:EHR35179.1, ECO:0000313|Proteomes:UP000003599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR35179.1,
RC   ECO:0000313|Proteomes:UP000003599};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dolosigranulum pigrum ATCC 51524.";
RL   Submitted (JAN-2012) 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:EHR35179.1}.
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DR   EMBL; AGEF01000001; EHR35179.1; -; Genomic_DNA.
DR   RefSeq; WP_004634530.1; NZ_JH601103.1.
DR   AlphaFoldDB; H3NBU6; -.
DR   PATRIC; fig|883103.3.peg.26; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   Proteomes; UP000003599; 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:UP000003599}.
FT   DOMAIN          21..352
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          464..585
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          386..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  67524 MW;  72E4938C85F6432D CRC64;
     MSLSYTNRQE ILSHLKNNEF DILIIGGGIT GAGLALQSAA SGLETGLIEM QDFSEGTSSR
     STKLVHGGIR YLKQFDVEVV NDTVGERAVV QQIAPHIPKP DPMLIPLYDE EGSTFDPFKL
     KVAMNLYDSL AGIDNTTLAN YSLSKEGTLK RVPGLMSEGL LGGGNYLDFN NSDVRLVIEN
     IKKAHEDGGT MASRVKAVDY LYNEEGNICG VRAEDVLTGE QFDIAAKVVV NASGPWSDKV
     RNLGREEEES FYQMRPTKGV HLVVDKERLT VPQPIYFDTG LGDGRMVFVI PREDKTFFGT
     TDTDYTGDYT TPKITQEDVD YLLDVVNRRF PDAHITLDDV ESSWAGLRPL ISGNAGSDYN
     GGDSGKISDE SFDNLVETVK QFINQDSSRD EVEEAVRSVE GQTSERDPSA VSRGSKLDVG
     ENGLVTIAGG KITDYRKMAE STLEKTIEIL ERDYDKFFHK INSKTYPVSG GQLDPENVDR
     EIERLIQRGI EKGLSPEDAA YLSNLYGSNA PQVFSLIDEV EPVEGLETKY LLSLHYALRN
     EMVISPVDFL VRRTNLMLFM RDKVDEVKEP LFAVMKEALG WSDEQEQAYR DELQETLDIN
     DLKYLR
//
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