NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0044-8486(01)00731-1; AGRICOLA=IND23320045
Nam Y.K., Cho Y.S., Douglas S.E., Gallant J.W., Reith M.E., Kim D.S.;
"Isolation and transient expression of a cDNA encoding L-gulono-g-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis, from the tiger shark Scyliorhinus torazame.";
Aquaculture 209:271-284(2002).

Comments

FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate (By similarity).
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 (By similarity).
PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis .
SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein (By similarity). Endoplasmic reticulum membrane; Single-pass membrane protein (By similarity).
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

AY039838; AAK73281.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q90YK3.

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: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).

Phylogenomic databases

HOVERGEN

Q90YK3; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 440`	`440`	`L-gulonolactone oxidase.`	`PRO_0000128162`
`TRANSMEM`	`245 267`	`23`	`Potential.`
`DOMAIN`	`17 187`	`171`	`FAD-binding PCMH-type.`
`MOD_RES`	`54 54`		`Tele-8alpha-FAD histidine (By similarity).`

Sequence information

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

Molecular weight: 50958 Da [This is the MW of the unprocessed precursor]

CRC64: F32FBBE69ACB03B7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQGTMGYQF ENWATTYSCE PELYFEPTTV EEIRQILELA NQRNKRVKVV GCGHSPSDIA 

        70         80         90        100        110        120 
CTDNYLVRLN KLNRILQVDK ERKWITAEAG ILLSDLNEKL DALGLALSNI GAVSDVALGG 

       130        140        150        160        170        180 
VIGTGTHNTG IQHGILATQI VAMTLMTAAG DTLECSNTVN REIFQATRLH LGSLGVVLNV 

       190        200        210        220        230        240 
TIQCVPAFRI HLQQFPKTLT EVLGDLDTHL KQSEYFRFFW FPHTDKVTVF YADRTNKPIK 

       250        260        270        280        290        300 
TTSSWFWNYA IGYYLLEFLL WISVFVPRLV PWINRLFYWL LYSAKAEQVK RSDKAFNFDC 

       310        320        330        340        350        360 
LFKQHVSDWA LPIKQTRAAL EQLKDWLDNN PNVRAHFPVE VRFVRADDIL LSPCYRQDSC 

       370        380        390        400        410        420 
YINIIMYRPY GKEVPREGYW AMYEEIMKRN GGRPHWAKAH SLLRQDFEKI YPAFHKFCSI 

       430        440 
REELDPSGMF LNNYLEKTFF

Q90YK3 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