GGLO_RAT
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 03-AUG-2022, entry version 168.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3338984; DOI=10.1016/s0021-9258(19)77923-x;
RA Koshizaka T., Nishikimi M., Ozawa T., Yagi K.;
RT "Isolation and sequence analysis of a complementary DNA encoding rat liver
RT 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 PubMed=1400507; DOI=10.1016/s0021-9258(19)36707-9;
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 this
RT species.";
RL J. Biol. Chem. 267:21967-21972(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1962571; DOI=10.1093/ajcn/54.6.1203s;
RA Nishikimi M., Yagi K.;
RT "Molecular basis for the deficiency in humans of gulonolactone oxidase, a
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-237.
RX 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 missing
RT 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 PubMed=8459881; DOI=10.1159/000187250;
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 L-
CC xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
CC {ECO:0000269|PubMed:8459881}.
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;
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; Single-pass membrane protein.
CC Endoplasmic reticulum membrane; Single-pass membrane protein.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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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 PIR; A45123; OXRTGU.
DR RefSeq; NP_071556.2; NM_022220.2.
DR AlphaFoldDB; P10867; -.
DR SMR; P10867; -.
DR IntAct; P10867; 1.
DR STRING; 10116.ENSRNOP00000022703; -.
DR iPTMnet; P10867; -.
DR PhosphoSitePlus; P10867; -.
DR PaxDb; P10867; -.
DR PRIDE; P10867; -.
DR GeneID; 60671; -.
DR KEGG; rno:60671; -.
DR UCSC; RGD:620701; rat.
DR CTD; 268756; -.
DR RGD; 620701; Gulo.
DR eggNOG; KOG4730; Eukaryota.
DR InParanoid; P10867; -.
DR OrthoDB; 1134169at2759; -.
DR PhylomeDB; P10867; -.
DR BioCyc; MetaCyc:MON-13235; -.
DR UniPathway; UPA00991; UER00939.
DR PRO; PR:P10867; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Ascorbate biosynthesis; Direct protein sequencing; Endoplasmic reticulum;
KW FAD; Flavoprotein; Membrane; Microsome; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8459881"
FT CHAIN 2..440
FT /note="L-gulonolactone oxidase"
FT /id="PRO_0000128161"
FT TRANSMEM 251..273
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"
FT CONFLICT 85
FT /note="I -> V (in Ref. 4; AAH89803)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="H -> Q (in Ref. 1; AAA41164)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="Q -> R (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
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
