Reviewed, UniProtKB/Swiss-Prot O93852 (ALO_CANAL)

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 (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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-erythroascorbic acid biosynthesis; D-erythro-ascorbic acid 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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D-arabinono-1,4-lactone oxidase activity Inferred from electronic annotation. Source: EC FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity 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	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O93852-1 [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 / IFO 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF031228 Genomic DNA. Translation: AAC98913.1. AACQ01000032 Genomic DNA. Translation: EAL00425.1.
RefSeq	XP_719313.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3638983.
Organism-specific databases
CGD	CAL0000083. ALO1.
Phylogenomic databases
OMA	O93852. DCLFSQF.
Enzyme and pathway databases
BRENDA	1.1.3.37. 1124.
Family and domain databases
InterPro	IPR007173. ALO. IPR016166. FAD-bd_2. IPR010031. FAD_lactone_oxidase. 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]
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:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)