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O93852 (ALO_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Synonyms:ALO
ORF Names:CaO19.7551
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. Note: Membrane-embedded By similarity.

Sequence similarities

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

Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentMembrane
Mitochondrion
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbiosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular response to oxidative stress

Inferred from mutant phenotype Ref.1. Source: CGD

cellular response to starvation

Inferred from mutant phenotype Ref.1. Source: CGD

filamentous growth

Inferred from mutant phenotype Ref.1. Source: CGD

filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype Ref.1. Source: CGD

filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype Ref.1. Source: CGD

pathogenesis

Inferred from mutant phenotype Ref.1. Source: CGD

water-soluble vitamin metabolic process

Inferred by curator PubMed 7957197. Source: CGD

   Cellular_componentmitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 7957197. Source: CGD

plasma membrane

Inferred from direct assay PubMed 19824013. Source: CGD

   Molecular_functionD-arabinono-1,4-lactone oxidase activity

Inferred from direct assay PubMed 7957197. Source: CGD

UDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557D-arabinono-1,4-lactone oxidase
PRO_0000128164

Regions

Domain25 – 209185FAD-binding PCMH-type

Amino acid modifications

Modified residue621Pros-8alpha-FAD histidine By similarity

Sequences

Sequence LengthMass (Da)Tools
O93852 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 0348233954111D92

FASTA55763,447
        10         20         30         40         50         60 
MTDIPESLKP FVTKKVIHST WAGTFLCKPQ AIFQPRNVEE IQELIKQARL HGKTIMTVGS 

        70         80         90        100        110        120 
GHSPSDLTMT TEWLCNLDKF NHVLLEEPYY APKSPTDDTP EIKFVDLTVE AGTRIFELNE 

       130        140        150        160        170        180 
YLKRNNLAIQ NLGSISDQSI AGLISTGTHG STQYHGLVSQ QVVSVKFLNS AGELITCSSV 

       190        200        210        220        230        240 
DKPEYFRAIL LSLGKIGIIT HVTLRTCPKY TIKSKQEIIN FETLLNNWDN LWLESEFIRI 

       250        260        270        280        290        300 
WWFPYTNKCV LWRANKSTDP LSDPRPSWYG TKLGRFFYES LLWVSVHLFP RLTPFVEKFV 

       310        320        330        340        350        360 
FGQQYGEVET LGKGDIAVQN SVEGLNMDCL FSQFVNEWSS PLNSGPEILT ELKKIITDAS 

       370        380        390        400        410        420 
QTGDFFVHAP IEVRCSNVTY SDEPFTDDKN QKSLYPSQEW LSNRSKTSAG PIPGNNLRPY 

       430        440        450        460        470        480 
LDNSPKLPYS KDGKITNDQL TLFINATMYR PFGTNVETHK WFQLFEDVMS KAGGKPHWAK 

       490        500        510        520        530        540 
NFIGLTQDEK YDKQQDLKTQ LEFGGKPFYT MLGFKPVMQD WFGKDLVAFN KVRKETDPDG 

       550 
VFLSGKVWAE RNGILLD 

« Hide

References

« Hide 'large scale' references
[1]"Deficiency of D-erythroascorbic acid attenuates hyphal growth and virulence of Candida albicans."
Huh W.-K., Kim S.-T., Kim H., Jeong G., Kang S.-O.
Infect. Immun. 69:3939-3946(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031228 Genomic DNA. Translation: AAC98913.1.
AACQ01000032 Genomic DNA. Translation: EAL00425.1.
RefSeqXP_719313.1. XM_714220.1.

3D structure databases

ProteinModelPortalO93852.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0000083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3638983.
KEGGcal:CaO19.7551.

Organism-specific databases

CGDCAL0000083. ALO1.

Phylogenomic databases

eggNOGCOG0277.
KOK00107.
OrthoDBEOG7JX3CZ.

Enzyme and pathway databases

UniPathwayUPA00771; UER00766.

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. SSF56176. 1 hit.
TIGRFAMsTIGR01678. FAD_lactone_ox. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALO_CANAL
AccessionPrimary (citable) accession number: O93852
Secondary accession number(s): Q5ACU1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names