ID   GGLO_SCYTO              Reviewed;         440 AA.
AC   Q90YK3;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=L-gulonolactone oxidase;
DE            Short=LGO;
DE            EC=1.1.3.8;
DE   AltName: Full=L-gulono-gamma-lactone oxidase;
DE            Short=GLO;
GN   Name=GULO;
OS   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes;
OC   Scyliorhinidae; Scyliorhinus.
OX   NCBI_TaxID=75743;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   AGRICOLA=IND23320045; DOI=10.1016/S0044-8486(01)00731-1;
RA   Nam Y.K., Cho Y.S., Douglas S.E., Gallant J.W., Reith M.E., Kim D.S.;
RT   "Isolation and transient expression of a cDNA encoding L-gulono-g-
RT   lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis, from
RT   the tiger shark Scyliorhinus torazame.";
RL   Aquaculture 209:271-284(2002).
CC   -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and
CC       L-xylo-hexulonolactone which spontaneously isomerizes to L-
CC       ascorbate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-gulono-1,4-lactone + O(2) = L-xylo-hex-2-
CC       ulono-1,4-lactone + H(2)O(2).
CC   -!- CATALYTIC ACTIVITY: L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbic acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Single-
CC       pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
CC       oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; AY039838; AAK73281.1; -; mRNA.
DR   HOVERGEN; Q90YK3; -.
DR   BRENDA; 1.1.3.8; 266735.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050105; F:L-gulonolactone oxidase activity; IEA:EC.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007173; ALO.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
DR   InterPro; IPR010031; FAD_lactone_oxidase.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Gene3D; G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   TIGRFAMs; TIGR01678; FAD_lactone_ox; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; Endoplasmic reticulum; FAD; Flavoprotein;
KW   Membrane; Microsome; Oxidoreductase; Transmembrane.
FT   CHAIN         1    440       L-gulonolactone oxidase.
FT                                /FTId=PRO_0000128162.
FT   TRANSMEM    245    267       Potential.
FT   DOMAIN       17    187       FAD-binding PCMH-type.
FT   MOD_RES      54     54       Tele-8alpha-FAD histidine (By
FT                                similarity).
SQ   SEQUENCE   440 AA;  50958 MW;  F32FBBE69ACB03B7 CRC64;
     MDQGTMGYQF ENWATTYSCE PELYFEPTTV EEIRQILELA NQRNKRVKVV GCGHSPSDIA
     CTDNYLVRLN KLNRILQVDK ERKWITAEAG ILLSDLNEKL DALGLALSNI GAVSDVALGG
     VIGTGTHNTG IQHGILATQI VAMTLMTAAG DTLECSNTVN REIFQATRLH LGSLGVVLNV
     TIQCVPAFRI HLQQFPKTLT EVLGDLDTHL KQSEYFRFFW FPHTDKVTVF YADRTNKPIK
     TTSSWFWNYA IGYYLLEFLL WISVFVPRLV PWINRLFYWL LYSAKAEQVK RSDKAFNFDC
     LFKQHVSDWA LPIKQTRAAL EQLKDWLDNN PNVRAHFPVE VRFVRADDIL LSPCYRQDSC
     YINIIMYRPY GKEVPREGYW AMYEEIMKRN GGRPHWAKAH SLLRQDFEKI YPAFHKFCSI
     REELDPSGMF LNNYLEKTFF
//