[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=3338984 [NCBI, ExPASy, EBI, Israel, Japan] Koshizaka T., Nishikimi M., Ozawa T., Yagi K.; "Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis."; J. Biol. Chem. 263:1619-1621(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; PubMed=1400507 [NCBI, ExPASy, EBI, Israel, Japan] Nishikimi M., Kawai T., Yagi K.; "Guinea pigs possess a highly mutated gene for L-gulono-gamma-lactone oxidase, the key enzyme for L-ascorbic acid biosynthesis missing in this species."; J. Biol. Chem. 267:21967-21972(1992).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1962571 [NCBI, ExPASy, EBI, Israel, Japan] Nishikimi M., Yagi K.; "Molecular basis for the deficiency in humans of gulonolactone oxidase, a key enzyme for ascorbic acid biosynthesis."; Am. J. Clin. Nutr. 54:1203S-1208S(1991).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-237. DOI=10.1016/0003-9861(88)90093-8; PubMed=3214183 [NCBI, ExPASy, EBI, Israel, Japan] Nishikimi M., Koshizaka T., Ozawa T., Yagi K.; "Occurrence in humans and guinea pigs of the gene related to their missing enzyme L-gulono-gamma-lactone oxidase."; Arch. Biochem. Biophys. 267:842-846(1988).
[6]	PROTEIN SEQUENCE OF 2-41, AND FUNCTION. PubMed=8459881 [NCBI, ExPASy, EBI, Israel, Japan] Fujitsuka N., Yokozawa T., Oura H., Akao T., Kobashi K., Ienaga K., Nakamura K.; "L-gulono-gamma-lactone oxidase is the enzyme responsible for the production of methylguanidine in the rat liver."; Nephron 63:445-451(1993).

Comments

FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
CATALYTIC ACTIVITY: L-gulono-1,4-lactone + O₂ = L-xylo-hex-2-ulono-1,4-lactone + H₂O₂.
CATALYTIC ACTIVITY: L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate.
COFACTOR: FAD.
PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis .
SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J03536; AAA41164.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D12754; BAA02232.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00526; BAA33497.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089803; AAH89803.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A45123; OXRTGU.

NP_071556.2; -.

3D structure databases

ModBase

P10867.

PTM databases

PhosphoSite

P10867; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13235; -.

Organism-specific databases

RGD

620701; Gulo.

Gene expression databases

ArrayExpress

P10867; -.

GermOnline

ENSRNOG00000016648; Rattus norvegicus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0003885;	Molecular function: D-arabinono-1,4-lactone oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0050105;	Molecular function: L-gulonolactone oxidase activity (inferred from electronic annotation from EC).
GO:0019853;	Biological process: L-ascorbic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007173; ALO.
IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR010031; FAD_lactone_oxidase.
IPR006094; Oxid_FAD_bind_N.
IPR006093; Oxy_OxRdtase_FAD_BS.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.

Pfam

PF04030; ALO; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01678; FAD_lactone_ox; 1.

PROSITE

PS51387; FAD_PCMH; 1.
PS00862; OX2_COVAL_FAD; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000016648; Rattus norvegicus. [Contig view]

GeneID

60671; -.

KEGG

rno:60671; -.

Phylogenomic databases

HOVERGEN

P10867; -.

Other

612407; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Ascorbate biosynthesis; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 440`	`439`	`L-gulonolactone oxidase.`	`PRO_0000128161`
`TRANSMEM`	`251 273`	`23`	`Potential.`
`DOMAIN`	`17 187`	`171`	`FAD-binding PCMH-type.`
`MOD_RES`	`54 54`		`Tele-8alpha-FAD histidine (By similarity).`
`CONFLICT`	`85 85`		`I -> V (in Ref. 4; AAH89803).`
`CONFLICT`	`189 189`		`H -> Q (in Ref. 1; AAA41164).`
`CONFLICT`	`404 404`		`Q -> R (in Ref. 2 and 4).`

Sequence information

Length: 440 AA [This is the length of the unprocessed precursor]

Molecular weight: 50615 Da [This is the MW of the unprocessed precursor]

CRC64: D63AD580A6F591F8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVHGYKGVQF QNWAKTYGCS PEVYYQPTSV EEVREVLALA REQKKKVKVV GGGHSPSDIA 

        70         80         90        100        110        120 
CTDGFMIHMG KMNRVLQVDK EKKQITVEAG ILLADLHPQL DEHGLAMSNL GAVSDVTVAG 

       130        140        150        160        170        180 
VIGSGTHNTG IKHGILATQV VALTLMTADG EVLECSESRN ADVFQAARVH LGCLGIILTV 

       190        200        210        220        230        240 
TLQCVPQFHL QETSFPSTLK EVLDNLDSHL KRSEYFRFLW FPHTENVSII YQDHTNKAPS 

       250        260        270        280        290        300 
SASNWFWDYA IGFYLLEFLL WTSTYLPCLV GWINRFFFWM LFNCKKESSN LSHKIFTYEC 

       310        320        330        340        350        360 
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC 

       370        380        390        400        410        420 
YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTQKDFEEM YPTFHKFCDI 

       430        440 
REKLDPTGMF LNSYLEKVFY

P10867 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools