ID   GGLO_RAT                Reviewed;         440 AA.
AC   P10867; Q5EBC1; Q64597; Q9QWR6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 87.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=88115275; PubMed=3338984;
RA   Koshizaka T., Nishikimi M., Ozawa T., Yagi K.;
RT   "Isolation and sequence analysis of a complementary DNA encoding rat
RT   liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid
RT   biosynthesis.";
RL   J. Biol. Chem. 263:1619-1621(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=93016162; PubMed=1400507;
RA   Nishikimi M., Kawai T., Yagi K.;
RT   "Guinea pigs possess a highly mutated gene for L-gulono-gamma-lactone
RT   oxidase, the key enzyme for L-ascorbic acid biosynthesis missing in
RT   this species.";
RL   J. Biol. Chem. 267:21967-21972(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92074404; PubMed=1962571;
RA   Nishikimi M., Yagi K.;
RT   "Molecular basis for the deficiency in humans of gulonolactone
RT   oxidase, a key enzyme for ascorbic acid biosynthesis.";
RL   Am. J. Clin. Nutr. 54:1203S-1208S(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-237.
RX   MEDLINE=89104405; PubMed=3214183; DOI=10.1016/0003-9861(88)90093-8;
RA   Nishikimi M., Koshizaka T., Ozawa T., Yagi K.;
RT   "Occurrence in humans and guinea pigs of the gene related to their
RT   missing enzyme L-gulono-gamma-lactone oxidase.";
RL   Arch. Biochem. Biophys. 267:842-846(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-41, AND FUNCTION.
RX   MEDLINE=93211519; PubMed=8459881;
RA   Fujitsuka N., Yokozawa T., Oura H., Akao T., Kobashi K., Ienaga K.,
RA   Nakamura K.;
RT   "L-gulono-gamma-lactone oxidase is the enzyme responsible for the
RT   production of methylguanidine in the rat liver.";
RL   Nephron 63:445-451(1993).
CC   -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and
CC       L-xylo-hexulonolactone which spontaneously isomerizes to L-
CC       ascorbate.
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.
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbic acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane
CC       protein. Endoplasmic reticulum membrane; Single-pass membrane
CC       protein.
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; J03536; AAA41164.1; -; Genomic_DNA.
DR   EMBL; D12754; BAA02232.1; -; Genomic_DNA.
DR   EMBL; D00526; BAA33497.1; -; Genomic_DNA.
DR   EMBL; BC089803; AAH89803.1; -; mRNA.
DR   IPI; IPI00555278; -.
DR   PIR; A45123; OXRTGU.
DR   RefSeq; NP_071556.2; -.
DR   UniGene; Rn.115212; -.
DR   PRIDE; P10867; -.
DR   Ensembl; ENSRNOG00000016648; Rattus norvegicus.
DR   GeneID; 60671; -.
DR   KEGG; rno:60671; -.
DR   RGD; 620701; Gulo.
DR   HOVERGEN; P10867; -.
DR   BioCyc; MetaCyc:MON-13235; -.
DR   BRENDA; 1.1.3.8; 248.
DR   NextBio; 612407; -.
DR   ArrayExpress; P10867; -.
DR   GermOnline; ENSRNOG00000016648; Rattus norvegicus.
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; TAS:RGD.
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; TAS:RGD.
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   1: Evidence at protein level;
KW   Ascorbate biosynthesis; Direct protein sequencing;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Oxidoreductase; Transmembrane.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    440       L-gulonolactone oxidase.
FT                                /FTId=PRO_0000128161.
FT   TRANSMEM    251    273       Potential.
FT   DOMAIN       17    187       FAD-binding PCMH-type.
FT   MOD_RES      54     54       Tele-8alpha-FAD histidine (By
FT                                similarity).
FT   CONFLICT     85     85       I -> V (in Ref. 4; AAH89803).
FT   CONFLICT    189    189       H -> Q (in Ref. 1; AAA41164).
FT   CONFLICT    404    404       Q -> R (in Ref. 2 and 4).
SQ   SEQUENCE   440 AA;  50615 MW;  D63AD580A6F591F8 CRC64;
     MVHGYKGVQF QNWAKTYGCS PEVYYQPTSV EEVREVLALA REQKKKVKVV GGGHSPSDIA
     CTDGFMIHMG KMNRVLQVDK EKKQITVEAG ILLADLHPQL DEHGLAMSNL GAVSDVTVAG
     VIGSGTHNTG IKHGILATQV VALTLMTADG EVLECSESRN ADVFQAARVH LGCLGIILTV
     TLQCVPQFHL QETSFPSTLK EVLDNLDSHL KRSEYFRFLW FPHTENVSII YQDHTNKAPS
     SASNWFWDYA IGFYLLEFLL WTSTYLPCLV GWINRFFFWM LFNCKKESSN LSHKIFTYEC
     RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC
     YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTQKDFEEM YPTFHKFCDI
     REKLDPTGMF LNSYLEKVFY
//