ID F2QFZ4_STROU Unreviewed; 608 AA.
AC F2QFZ4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 Name=glpD {ECO:0000313|EMBL:CBZ01563.1};
GN OrderedLocusNames=SOR_1916 {ECO:0000313|EMBL:CBZ01563.1};
OS Streptococcus oralis (strain Uo5).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=927666 {ECO:0000313|EMBL:CBZ01563.1, ECO:0000313|Proteomes:UP000008131};
RN [1] {ECO:0000313|EMBL:CBZ01563.1, ECO:0000313|Proteomes:UP000008131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uo5 {ECO:0000313|EMBL:CBZ01563.1,
RC ECO:0000313|Proteomes:UP000008131};
RX PubMed=21460080; DOI=10.1128/JB.00321-11;
RA Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B., Maurer P.,
RA Rieger M., Klages S., Reinhard R., Hakenbeck R.;
RT "Genome of Streptococcus oralis strain Uo5.";
RL J. Bacteriol. 193:2888-2889(2011).
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; FR720602; CBZ01563.1; -; Genomic_DNA.
DR RefSeq; WP_000395897.1; NC_015291.1.
DR AlphaFoldDB; F2QFZ4; -.
DR KEGG; sor:SOR_1916; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_2_9; -.
DR Proteomes; UP000008131; Chromosome.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBZ01563.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..350
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"
FT REGION 393..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 66713 MW; 19554239087E6A56 CRC64;
MEFSKKTREL SIKKMQERTL DLLIIGGGIT GAGVALQAAA SGLDTGLIEM QDFAEGTSSR
STKLVHGGLR YLKQFDVEVV SDTVSERAVV QQIAPHIPKP DPMLLPVYDE DGATFSLFRL
KVAMDLYDLL AGVSNTPAAN KVLSKEEVLE RQPNLKKEGL VGGGVYLDFR NNDARLVIEN
IKRANQDGAL IANHVRAEGF LFDESGKITG VVARDLLTDQ VFEIKARLVI NTTGPWSDKV
RNLSNKGTQF SQMRPTKGVH LVVDSSKIKV SQPVYFDTGL GDGRMVFVLP RENKTYFGTT
DTDYTGDLEH PKVTQEDVDY LLGIVNNRFS EANITIDDIE SSWAGLRPLI AGNSASDYNG
GNNGTISDES FNNLIATVEA YLSKEKTRED VESAVSKLES STSEKHLDPS AVSRGSSLDR
DDNGLLTLAG GKITDYRKMA EGAMERVVDI LKAEFDRSFK LINSKTYPVS GGELNPANVD
SEIEAFAQLG VSRGLDSKEA HYLANLYGSN APKVFALAHS LEQAPGLSLA DTLSLHYAMR
NELALSPVDF LLRRTNHMLF MRDSLDSIVE PVLDEMGRFY DWTEEEKAAY HADVEAALAQ
NDLAELKN
//
