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P54783 (ALO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-arabinono-1,4-lactone oxidase
Short name=ALO
EC=1.1.3.37
Alternative name(s):
L-galactono-gamma-lactone oxidase
Gene names
Name:ALO1
Ordered Locus Names:YML086C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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-erythroascorbate biosynthesis; dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2.

Subcellular location

Mitochondrion membrane. Note: Membrane-embedded.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

Present with 6190 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the oxygen-dependent FAD-linked oxidoreductase family.

Contains 1 FAD-binding PCMH-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-2519,EBI-2519
ACB1P317871EBI-2519,EBI-2060
ADE17P380091EBI-2519,EBI-14223
ARF1P110761EBI-2519,EBI-2816
ARO8P530901EBI-2519,EBI-2042933
CWP2P434971EBI-2519,EBI-2044078
CYS4P325821EBI-2519,EBI-4167
DAP1Q120911EBI-2519,EBI-5554
DBP5P204491EBI-2519,EBI-5617
DNM1P548611EBI-2519,EBI-6002
EHT1P382951EBI-2519,EBI-20890
FAA3P390021EBI-2519,EBI-10089
FUN14P184111EBI-2519,EBI-20609
GLN1P322881EBI-2519,EBI-7665
GTT1P405821EBI-2519,EBI-7941
HSP12P229431EBI-2519,EBI-8548
HUG1Q6Q5K61EBI-2519,EBI-392766
HYR1P405811EBI-2519,EBI-7869
IML2P470311EBI-2519,EBI-25966
INO1P119861EBI-2519,EBI-9257
IPP1P008171EBI-2519,EBI-9338
KES1P358441EBI-2519,EBI-9648
LSP1Q122301EBI-2519,EBI-34978
MCR1P360601EBI-2519,EBI-10565
MSP1P287371EBI-2519,EBI-11435
OYE2Q035581EBI-2519,EBI-12729
PCK1P109631EBI-2519,EBI-13770
PGM2P370121EBI-2519,EBI-13296
PMP3P872841EBI-2519,EBI-13555
QCR9P222891EBI-2519,EBI-19947
RNR1P215241EBI-2519,EBI-15234
RNR2P099381EBI-2519,EBI-15240
SAH1P399541EBI-2519,EBI-16451
SAM35P146931EBI-2519,EBI-24602
SEC4P075601EBI-2519,EBI-16858
SIS1P252941EBI-2519,EBI-17244
SNC2P333281EBI-2519,EBI-17512
SNF7P399291EBI-2519,EBI-17554
SSL2Q005781EBI-2519,EBI-14683
TOM20P351801EBI-2519,EBI-12522
TOM70P072131EBI-2519,EBI-12551
TSC10P383421EBI-2519,EBI-21124
UIP4Q089261EBI-2519,EBI-2044051
URA7P282741EBI-2519,EBI-20128
VAS1P07806-11EBI-2519,EBI-1009942From a different organism.
YBL039W-BP0C2681EBI-2519,EBI-2044092
YDR381C-AQ3E6R51EBI-2519,EBI-2044020
YGR012WP532061EBI-2519,EBI-2044073
YHR003CP387561EBI-2519,EBI-24431
YHR146WP388451EBI-2519,EBI-24770
YPT1P011231EBI-2519,EBI-29496
YPT31P385551EBI-2519,EBI-29379
YPT32P519961EBI-2519,EBI-29384

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526D-arabinono-1,4-lactone oxidase
PRO_0000128171

Regions

Domain19 – 193175FAD-binding PCMH-type

Amino acid modifications

Modified residue561Pros-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict4171A → P in BAA23804. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P54783 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 942177A74A738EC8

FASTA52659,494
        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

« Hide

References

« Hide 'large scale' references
[1]"D-erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae."
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.
Mol. Microbiol. 30:895-903(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 86-105 AND 349-363.
Strain: ATCC 44774 / DBY747.
[2]"Identification of the yeast genomic sequence encoding L-galactono-gamma-lactone oxidase."
Nishikimi M., Ohata Y., Ishikawa T.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
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. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U40390 Genomic DNA. Translation: AAC98538.1.
AB009401 Genomic DNA. Translation: BAA23804.1.
Z46660 Genomic DNA. Translation: CAA86652.1.
AY693120 Genomic DNA. Translation: AAT93139.1.
BK006946 Genomic DNA. Translation: DAA09811.1.
PIRS49641.
RefSeqNP_013624.1. NM_001182445.1.

3D structure databases

ProteinModelPortalP54783.
SMRP54783. Positions 14-204.
ModBaseSearch...

Protein-protein interaction databases

IntActP54783. 39 interactions.
MINTMINT-4497062.

Proteomic databases

PaxDbP54783.
PeptideAtlasP54783.

Protocols and materials databases

DNASU854888.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML086C; YML086C; YML086C.
GeneID854888.
KEGGsce:YML086C.

Organism-specific databases

CYGDYML086c.
SGDS000004551. ALO1.

Phylogenomic databases

eggNOGCOG0277.
GeneTreeENSGT00510000049722.
HOGENOMHOG000204635.
KOK00107.
OMADCLFSQF.
OrthoDBEOG4GF6PD.

Enzyme and pathway databases

UniPathwayUPA00771; UER00766.

Gene expression databases

GenevestigatorP54783.
GermOnlineYML086C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProIPR007173. ALO.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR010031. FAD_lactone_oxidase.
IPR023595. LGO_GLO.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamPF04030. ALO. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PIRSFPIRSF000136. LGO_GLO. 1 hit.
SUPFAMSSF56176. FAD-binding_2. 1 hit.
TIGRFAMsTIGR01678. FAD_lactone_ox. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977843.

Entry information

Entry nameALO_YEAST
AccessionPrimary (citable) accession number: P54783
Secondary accession number(s): D6W0J7, O42618
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents