D-arabinono-1,4-lactone oxidase - Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

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O93852 (ALO_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Virulence
Cellular component	Membrane Mitochondrion
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	biosynthetic 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 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_component	mitochondrial 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_function	D-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 557

557

D-arabinono-1,4-lactone oxidase

PRO_0000128164

Regions

Domain

25 – 209

185

FAD-binding PCMH-type

Amino acid modifications

Modified residue

Pros-8alpha-FAD histidine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O93852 [UniParc].

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

FASTA

557

63,447

        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' referencesShow '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.
RefSeq	XP_719313.1. XM_714220.1.
3D structure databases
ProteinModelPortal	O93852.
ModBase	Search...
Protein-protein interaction databases
STRING	5476.CAL0000083.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3638983.
KEGG	cal:CaO19.7551.
Organism-specific databases
CGD	CAL0000083. ALO1.
Phylogenomic databases
eggNOG	COG0277.
KO	K00107.
Enzyme and pathway databases
UniPathway	UPA00771; UER00766.
Family and domain databases
Gene3D	3.30.43.10. 1 hit. 3.30.465.10. 1 hit.
InterPro	IPR007173. 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]
Pfam	PF04030. ALO. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
PIRSF	PIRSF000136. LGO_GLO. 1 hit.
SUPFAM	SSF56176. FAD-binding_2. 1 hit.
TIGRFAMs	TIGR01678. FAD_lactone_ox. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. PS00862. OX2_COVAL_FAD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALO_CANAL

Accession

Primary (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 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents