ID C9A595_ENTCA Unreviewed; 609 AA.
AC C9A595;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, 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 ORFNames=ECBG_00056 {ECO:0000313|EMBL:EEV37787.1};
OS Enterococcus casseliflavus EC20.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV37787.1, ECO:0000313|Proteomes:UP000012675};
RN [1] {ECO:0000313|EMBL:EEV37787.1, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV37787.1,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genome Sequencing Platform;
RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEV37787.1, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV37787.1,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL Submitted (MAR-2013) 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}.
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DR EMBL; CP004856; EEV37787.1; -; Genomic_DNA.
DR RefSeq; WP_015509063.1; NZ_AKCC01000001.1.
DR AlphaFoldDB; C9A595; -.
DR GeneID; 15141274; -.
DR KEGG; ecas:ECBG_00056; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_2_9; -.
DR Proteomes; UP000012675; 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 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:UP000012675}.
FT DOMAIN 21..351
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 465..583
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 609 AA; 67237 MW; FD5AAEABCEE01476 CRC64;
MTFSHKDRKQ TIQEAAKTTY DVLIIGGGIT GAGVAVQTAA AGMKTVLLEM QDFAEGTSSR
STKLVHGGIR YLKTFDVEVV ADTVRERAIV QQIAPHIPKP DPMLLPIYDE PGATFSLFSV
KVAMDLYDRL ANVTGSKYEN YLLTKEEVLE REPQLQAENL VGGGVYLDFR NNDARLVIEN
IKRAQADGAA MISKAKVVGI LHDEQGIING VEVEDQLTNE RFEVHAKVVI NTTGPWSDIV
RQLDKNDELP PQMRPTKGVH LVVDREKLKV PQPTYFDTGK NDGRMVFVVP RENKTYFGTT
DTDYTGDFAH PTVTQEDVDY LLTIVNERFP HAQITLDDIE ASWAGLRPLI VNNGGSDYNG
GGKGKLSDES FEQIVESVKE YLEDERQRPV VEKAVKQAQE RVEASKVDPS QVSRGSSLER
SKDGLLTLAG GKITDYRLMA EGAVKRINEL LQESGASFEL VDSTTYPVSG GELDAANVEE
DLAKLADQAQ AAGFDEAAAT YLAHLYGSNL PQVLNYKTKF EGLDEKESTA LNYSLHEEMV
LTPVDYLLRR TNHILFMRDT LDEVKAGVVA AMTDFFGWSE EEKAAHVAEL NQVIAESDLT
ALKGGKKDE
//
