O93852 (ALO_CANAL) Reviewed, UniProtKB/Swiss-Prot

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)

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
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 hyphal growth 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. Source: CGD
Cellular component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: CGD
Molecular function	D-arabinono-1,4-lactone oxidase activity Inferred from direct assay. 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	62	1	Pros-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O93852 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 0348233954111D92	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

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: 11349062] [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: 15123810] [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...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3638983.
KEGG	cal:CaO19.7551.
Organism-specific databases
CGD	CAL0000083. ALO1.
Phylogenomic databases
OMA	DCLFSQF.
PhylomeDB	O93852.
Family and domain databases
InterPro	IPR007173. ALO. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR010031. FAD_lactone_oxidase. IPR023595. LGO_GLO. IPR006094. Oxid_FAD_bind_N. IPR006093. Oxy_OxRdtase_FAD_BS. [Graphical view]
Gene3D	G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
KO	K00107.
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:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program