[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 86-105 AND 349-363. STRAIN=ATCC 44774 / DBY747; DOI=10.1046/j.1365-2958.1998.01133.x; PubMed=10094636 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Lee B.-H., Kim S.-T., Kim Y.-R., Rhie G.-E., Baek Y.-W., Hwang C.-S., Lee J.-S., Kang S.-O.; "D-erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae."; Mol. Microbiol. 30:895-903(1998).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Nishikimi M., Ohata Y., Ishikawa T.; "Identification of the yeast genomic sequence encoding L-galactono-gamma-lactone oxidase."; Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[5]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).

Comments

FUNCTION: Can oxidize L-gulono-1,4-lactone as well as D-arabinono-1,4-lactone and L-galactono-1,4-lactone.
CATALYTIC ACTIVITY: D-arabinono-1,4-lactone + O₂ = dehydro-D-arabinono-1,4-lactone + H₂O₂.
COFACTOR: FAD.
PATHWAY: Cofactor biosynthesis; D-erythroascorbic acid biosynthesis; D-erythro-ascorbic acid from D-arabinose: step 2/2 .
SUBCELLULAR LOCATION: Mitochondrion membrane. Note=Membrane-embedded.
PTM: The N-terminus is blocked.
MISCELLANEOUS: Present with 6190 molecules/cell in log phase SD medium.
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

U40390; AAC98538.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009401; BAA23804.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46660; CAA86652.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY693120; AAT93139.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S49641; S49641.

RefSeq

NP_013624.1; -.

3D structure databases

ModBase

P54783.

Organism-specific databases

YML086c; -.

S000004551; ALO1.

Gene expression databases

GermOnline

YML086C; Saccharomyces cerevisiae.

Ontologies

GO:0031307;	Cellular component: integral to mitochondrial outer membrane (inferred from direct assay from SGD).
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:0009058;	Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR007173; ALO.
IPR010031; FAD_lactone_oxidase.
IPR006094; Oxid_FAD_bind_N.
IPR006093; Oxy_OxRdtase_FAD_BS.
Graphical view of domain structure.

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).

Proteomic databases

PeptideAtlas

P54783; -.

Genome annotation databases

Ensembl

YML086C; Saccharomyces cerevisiae. [Contig view]

854888; -.

Z71257_GR; YML086C.

sce:YML086C; -.

fig|4932.3.peg.4661; -.

Phylogenomic databases

HOGENOM

P54783; -.

Other

P54783; -.

977843; -.

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

Keywords

Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 526`	`526`	`D-arabinono-1,4-lactone oxidase.`	`PRO_0000128171`
`DOMAIN`	`19 193`	`175`	`FAD-binding PCMH-type.`
`MOD_RES`	`56 56`		`Tele-8alpha-FAD histidine (By similarity).`
`CONFLICT`	`417 417`		`A -> P (in Ref. 2; BAA23804).`

Sequence information

Length: 526 AA [This is the length of the unprocessed precursor]

Molecular weight: 59494 Da [This is the MW of the unprocessed precursor]

CRC64: 942177A74A738EC8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTIPFRKNY VFKNWAGIYS AKPERYFQPS SIDEVVELVK SARLAEKSLV TVGSGHSPSN 

        70         80         90        100        110        120 
MCVTDEWLVN LDRLDKVQKF VEYPELHYAD VTVDAGMRLY QLNEFLGAKG YSIQNLGSIS 

       130        140        150        160        170        180 
EQSVAGIIST GSHGSSPYHG LISSQYVNLT IVNGKGELKF LDAENDPEVF KAALLSVGKI 

       190        200        210        220        230        240 
GIIVSATIRV VPGFNIKSTQ EVITFENLLK QWDTLWTSSE FIRVWWYPYT RKCVLWRGNK 

       250        260        270        280        290        300 
TTDAQNGPAK SWWGTKLGRF FYETLLWIST KIYAPLTPFV EKFVFNRQYG KLEKSSTGDV 

       310        320        330        340        350        360 
NVTDSISGFN MDCLFSQFVD EWGCPMDNGL EVLRSLDHSI AQAAINKEFY VHVPMEVRCS 

       370        380        390        400        410        420 
NTTLPSEPLD TSKRTNTSPG PVYGNVCRPF LDNTPSHCRF APLENVTNSQ LTLYINATIY 

       430        440        450        460        470        480 
RPFGCNTPIH KWFTLFENTM MVAGGKPHWA KNFLGSTTLA AGPVKKDTDY DDFEMRGMAL 

       490        500        510        520 
KVEEWYGEDL KKFRKIRKEQ DPDNVFLANK QWAIINGIID PSELSD

P54783 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