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Database: UniProt
Entry: O86963
LinkDB: O86963
Original site: O86963 
ID   GLPO_ENTCA              Reviewed;         609 AA.
AC   O86963;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 85.
DE   RecName: Full=Alpha-glycerophosphate oxidase;
DE            EC=1.1.3.21;
DE   AltName: Full=Glycerol-3-phosphate oxidase;
GN   Name=glpO;
OS   Enterococcus casseliflavus (Enterococcus flavescens).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=37734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13 AND
RP   295-327, CHARACTERIZATION, AND MASS SPECTROMETRY.
RC   STRAIN=ATCC 12755 / DSM 4841 / NCFB 2725;
RX   PubMed=9726992; DOI=10.1074/jbc.273.37.23812;
RA   Parsonage D., Luba J., Mallett T.C., Claiborne A.;
RT   "The soluble alpha-glycerophosphate oxidase from Enterococcus
RT   casseliflavus. Sequence homology with the membrane-associated
RT   dehydrogenase and kinetic analysis of the recombinant enzyme.";
RL   J. Biol. Chem. 273:23812-23822(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642;
CC         EC=1.1.3.21;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MASS SPECTROMETRY: Mass=67082; Method=Electrospray; Range=2-609;
CC       Evidence={ECO:0000269|PubMed:9726992};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; U57498; AAC34739.1; -; Genomic_DNA.
DR   ProteinModelPortal; O86963; -.
DR   SMR; O86963; -.
DR   PRIDE; O86963; -.
DR   eggNOG; ENOG4105C6V; Bacteria.
DR   eggNOG; COG0578; LUCA.
DR   SABIO-RK; O86963; -.
DR   UniPathway; UPA00940; -.
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   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.8.870; -; 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; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW   Glycerol metabolism; Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:9726992}.
FT   CHAIN         2    609       Alpha-glycerophosphate oxidase.
FT                                /FTId=PRO_0000126107.
FT   NP_BIND      21     49       FAD. {ECO:0000255}.
SQ   SEQUENCE   609 AA;  67216 MW;  38A17281C16990F6 CRC64;
     MTFSQKDRKE TIQETAKTTY DVLIIGGGIT GAGVAVQTAA AGMKTVLLEM QDFAEGTSSR
     STKLVHGGIR YLKTFDVEVV ADTVRERAIV QQIAPHIPKP DPMLLPIYDE PGATFSLFSV
     KVAMDLYDRL ANVTGSKYEN YLLTKEEVLA REPQLQAENL VGGGVYLDFR NNDARLVIEN
     IKRAQADGAA MISKAKVVGI LHDEQGIING VEVEDQLTNE RFEVHAKVVI NTTGPWSDIV
     RQLDKNDELP PQMRPTKGVH LVVDREKLKV PQPTYFDTGK NDGRMVFVVP RENKTYFGTT
     DTDYTGDFAH PTVTQEDVDY LLTIVNERFP HAQITLDDIE ASWAGLRPLI TNNGGSDYNG
     GGKGKLSDES FEQIVESVKE YLADERQRPV VEKAVKQAQE RVEASKVDPS QVSRGSSLER
     SKDGLLTLAG GKITDYRLMA EGAVKRINEL LQESGASFEL VDSTTYPVSG GELDAANVEE
     ELAKLADQAQ TAGFNEAAAT YLAHLYGSNL PQVLNYKTKF EGLDEKESTA LNYSLHEEMV
     LTPVDYLLRR TNHILFMRDT LDDVKAGVVA AMTDFFGWSE EEKAAHVLEL NQVIAESDLT
     ALKGGKKDE
//
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