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   03-AUG-2022, entry version 101.
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; Scyliorhinidae;
OC   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-lactone
RT   oxidase, a key enzyme for L-ascorbic acid biosynthesis, from the tiger
RT   shark Scyliorhinus torazame.";
RL   Aquaculture 209:271-284(2002).
CC   -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-
CC       xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC         Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-
CC       D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step
CC       4/4.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AY039838; AAK73281.1; -; mRNA.
DR   AlphaFoldDB; Q90YK3; -.
DR   SMR; Q90YK3; -.
DR   PRIDE; Q90YK3; -.
DR   BRENDA; 1.1.3.8; 5642.
DR   UniPathway; UPA00991; UER00939.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR   GO; GO:0050105; F:L-gulonolactone oxidase activity; ISS:UniProtKB.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR007173; ALO_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR010031; FAD_lactone_oxidase.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   InterPro; IPR030654; Sugar_lactone_oxidase.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR43762; PTHR43762; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PIRSF; PIRSF000136; LGO_GLO; 1.
DR   SUPFAM; SSF56176; SSF56176; 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; Membrane;
KW   Microsome; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..440
FT                   /note="L-gulonolactone oxidase"
FT                   /id="PRO_0000128162"
FT   TRANSMEM        245..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..187
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         54
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
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