ID A2RK82_LACLM Unreviewed; 525 AA.
AC A2RK82;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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:CAL97692.1};
GN OrderedLocusNames=llmg_1098 {ECO:0000313|EMBL:CAL97692.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870 {ECO:0000313|EMBL:CAL97692.1, ECO:0000313|Proteomes:UP000000364};
RN [1] {ECO:0000313|EMBL:CAL97692.1, ECO:0000313|Proteomes:UP000000364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363 {ECO:0000313|EMBL:CAL97692.1,
RC ECO:0000313|Proteomes:UP000000364};
RX PubMed=17307855; DOI=10.1128/JB.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL97692.1; -; Genomic_DNA.
DR RefSeq; WP_011835006.1; NZ_WJVF01000012.1.
DR AlphaFoldDB; A2RK82; -.
DR SMR; A2RK82; -.
DR STRING; 416870.llmg_1098; -.
DR KEGG; llm:llmg_1098; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_4_1_9; -.
DR OrthoDB; 9766796at2; -.
DR PhylomeDB; A2RK82; -.
DR Proteomes; UP000000364; 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 PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAL97692.1}.
FT DOMAIN 20..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 399..506
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 525 AA; 58580 MW; F479828003AA0D26 CRC64;
MSISRQKNIE YLKANPDDWD FIIIGGGATG LGVAVDAASR GYKTVLVEQS DFAKSTSSRS
TKLVHGGVRY LAQGDVSLVR EALHERGRLA RNAPHLVKNQ KFIIANYKAW EQPFYSIGMK
MYDALAGKLN IGKSKIYSKK KVAEAIPQIK HEHLVGGVMY YDGQFDDARM AINLMQTATE
QGALLVNYVK VTELVKTDSK VSSVKLHDEL SGESFELHGK AIINATGIFV DQIMSMDTKE
HKPSVRPSQG VHLIVDGSFL GGQDAIMVPK TSDGRVLFCV PWHNKVILGT TDTPLTEFVL
EPRPLEEEID FILETAGQYL EKKPERKDVL TAYAGLRPLA APKEGDGEKT KEISRSHKLF
TSESGLVTIT GGKWTTYRQM AEETVDLAIK TSKLPEKKCI TRTLKIHGAK ETTERERQNW
LYVYGSDKGK ILALQNEDSS LALPLHPKYE FTGSEVIWAV REEMAQTLDD VLARRIRALF
LDARIAKEMA PKVAQLMSKE MGKDEAWEKE QVESFLTLAD GYILK
//
