ID   GGLO_PIG                Reviewed;         440 AA.
AC   Q8HXW0; Q9N1U4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 47.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=15112110; DOI=10.1007/s00335-003-2324-6;
RA   Hasan L., Voegeli P., Stoll P., Kramer S.S., Stranzinger G.,
RA   Neuenschwander S.;
RT   "Intragenic deletion in the gene encoding L-gulonolactone oxidase
RT   causes vitamin C deficiency in pigs.";
RL   Mamm. Genome 15:323-333(2004).
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; AF440259; AAN63634.1; -; mRNA.
DR   EMBL; AF136938; AAF61429.1; -; mRNA.
DR   RefSeq; NP_001123420.1; -.
DR   UniGene; Ssc.16369; -.
DR   GeneID; 396759; -.
DR   KEGG; ssc:396759; -.
DR   HOVERGEN; Q8HXW0; -.
DR   BRENDA; 1.1.3.8; 249.
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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    440       L-gulonolactone oxidase.
FT                                /FTId=PRO_0000128160.
FT   TRANSMEM    253    273       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;  50352 MW;  81BC3E0873627201 CRC64;
     MVHGHKGVKF QNWAKTYGCC PEMYYQPTSV EEIREVLALA RQQNKRVKVV GGGHSPSDIA
     CTDGFMIHMG KMNRVLKVDM EKKQVTVEAG ILLADLHPQL DKHGLALSNL GAVSDVTAGG
     VIGSGTHNTG IKHGILATQV VELTLLTPDG TVLVCSESSN AEVFQAARVH LGCLGVILTV
     TLQCVPQFHL QETTFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSVI YQDHTNKPPS
     SSANWFWDYA IGFYLLEFLL WISTFVPGLV GWINRFFFWL LFNGKKENCN LSHKIFTYEC
     RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRADDIL LSPCFQRDSC
     YMNIIMYRPY GKDVPRLDYW LAYETIMKKV GGRPHWAKAH NCTRKDFEKM YPAFRKFCAI
     REKLDPTGMF LNAYLEKVFY
//