GGLO_PIG
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 03-AUG-2022, entry version 121.
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 {ECO:0000312|EMBL:AAN63634.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN63634.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAN63634.1};
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 causes
RT vitamin C deficiency in pigs.";
RL Mamm. Genome 15:323-333(2004).
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|UniProtKB:P10867}.
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 Evidence={ECO:0000250|UniProtKB:P10867};
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:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF440259; AAN63634.1; -; mRNA.
DR EMBL; AF136938; AAF61429.1; -; mRNA.
DR RefSeq; NP_001123420.1; NM_001129948.1.
DR AlphaFoldDB; Q8HXW0; -.
DR SMR; Q8HXW0; -.
DR STRING; 9823.ENSSSCP00000010324; -.
DR PaxDb; Q8HXW0; -.
DR PRIDE; Q8HXW0; -.
DR Ensembl; ENSSSCT00000010600; ENSSSCP00000010324; ENSSSCG00000009667.
DR Ensembl; ENSSSCT00015027517; ENSSSCP00015010775; ENSSSCG00015020623.
DR Ensembl; ENSSSCT00025031071; ENSSSCP00025013070; ENSSSCG00025022882.
DR Ensembl; ENSSSCT00030010253; ENSSSCP00030004400; ENSSSCG00030007623.
DR Ensembl; ENSSSCT00040096436; ENSSSCP00040042831; ENSSSCG00040070225.
DR Ensembl; ENSSSCT00045033137; ENSSSCP00045022966; ENSSSCG00045019385.
DR Ensembl; ENSSSCT00055033926; ENSSSCP00055026962; ENSSSCG00055017147.
DR Ensembl; ENSSSCT00060081888; ENSSSCP00060035476; ENSSSCG00060059995.
DR Ensembl; ENSSSCT00070045965; ENSSSCP00070038754; ENSSSCG00070023067.
DR GeneID; 396759; -.
DR KEGG; ssc:396759; -.
DR CTD; 268756; -.
DR VGNC; VGNC:109148; GULO.
DR eggNOG; KOG4730; Eukaryota.
DR GeneTree; ENSGT00510000049722; -.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; Q8HXW0; -.
DR OrthoDB; 1134169at2759; -.
DR TreeFam; TF328994; -.
DR UniPathway; UPA00991; UER00939.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000009667; Expressed in liver and 8 other tissues.
DR ExpressionAtlas; Q8HXW0; baseline.
DR Genevisible; Q8HXW0; SS.
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_0000128160"
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; 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
