ID   GGLO_BOVIN              Reviewed;         440 AA.
AC   Q3ZC33;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 123.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Rumen reticulum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102936; AAI02937.1; -; mRNA.
DR   RefSeq; NP_001029215.1; NM_001034043.2.
DR   AlphaFoldDB; Q3ZC33; -.
DR   SMR; Q3ZC33; -.
DR   STRING; 9913.ENSBTAP00000037993; -.
DR   PaxDb; Q3ZC33; -.
DR   PRIDE; Q3ZC33; -.
DR   Ensembl; ENSBTAT00000038177; ENSBTAP00000037993; ENSBTAG00000026748.
DR   GeneID; 286812; -.
DR   KEGG; bta:286812; -.
DR   CTD; 268756; -.
DR   VEuPathDB; HostDB:ENSBTAG00000026748; -.
DR   VGNC; VGNC:108931; GULO.
DR   eggNOG; KOG4730; Eukaryota.
DR   GeneTree; ENSGT00510000049722; -.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q3ZC33; -.
DR   OMA; YPRFGEF; -.
DR   OrthoDB; 1134169at2759; -.
DR   TreeFam; TF328994; -.
DR   UniPathway; UPA00991; UER00939.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000026748; Expressed in liver and 94 other tissues.
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: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   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Microsome; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..440
FT                   /note="L-gulonolactone oxidase"
FT                   /id="PRO_0000231673"
FT   TRANSMEM        253..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"
SQ   SEQUENCE   440 AA;  50282 MW;  8AAEE8413A80F048 CRC64;
     MVHGYKGVKF QNWARTYGCC PEMYFQPTSV EEVREVLALA RQQNKRVKVV GGGHSPSDIA
     CTDGFMIHMG KMNRVLKVDT EKKQVTVEAG ILLADLHPQL DKHGLALSNL GAVSDVTAGG
     VIGSGTHNTG IKHGILATQV VALTLLTANG TILECSESSN AEVFQAARVH LGCLGVILTV
     TLQCVPQFHL QETTFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSVI YQDHTNKPPS
     SSANWFWDYA IGFYLLEFLL WISTFLPGLV GWINRFFFWL LFNGKKENCN LSHKIFTYEC
     RFKQHVQDWA IPREKTKEAL LELKAMLEAN PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC
     YMNIIMYRPY GKDVPRLDYW LAYETIMKKV GGRPHWAKAH NCTRKDFEKM YPAFQRFCAI
     REKLDPTGMF LNAYLEKVFY