Reviewed, UniProtKB/Swiss-Prot Q6CG88 (ALO_YARLI)

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
Ordered Locus Names:	YALI0A21263g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	526 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 By similarity.
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
Cellular component	Membrane Mitochondrion
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 526	526	D-arabinono-1,4-lactone oxidase		PRO_0000128170
Regions
	Domain	22 – 196	175	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	59	1	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CG88-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 19AC25D2944948A1	FASTA	526	58,900
	10 20 30 40 50 60 MSLRNSTTAK RFHSHKTWAG TFWSRPSLYF QPASIEELQA IVTRARDLGK TIMVVGSAHS 70 80 90 100 110 120 PSDLTMTSQW LVNLDKLSKA VSFKPHTSGL YTDVTVEAGI RIHQLNEVLK RKGLAMQNLG 130 140 150 160 170 180 SISDQSVAGI ISTGTHGSSA YHGLVSQQIV SLTIMIASGE LLTCSPDENP TLFRAALLSL 190 200 210 220 230 240 GKLGIIVYAT LRTVPAYTIH STQHVITFET LIREWDNLWT ASEYIRVWWF PYAERCILWR 250 260 270 280 290 300 ASKSELPLSA PRPSWYGTWL GRLFYETLLW VSVRLWPSLT PSVERFIFSR QYGMEDTLGS 310 320 330 340 350 360 GTGSEAVQGS VEGLNMDCLF SQFVNEWGMP LDNGPDVLRA LRAKIEAAAK DNIYYVHSPV 370 380 390 400 410 420 EVRCSNMSVP DSGDRNVEPN TQEFSASRRG AITGNTLRPL LDINPRDRPY ASPHGHVTNS 430 440 450 460 470 480 NLTLYINATM YRPFGVNSPV GKWYRDFEGI VAEAGGKPHW AKNFLGPETA ELKDNESEDG 490 500 510 520 KMLGLKPIID EWYGDDLKQW KSLREKYDPT GVFLSGKVWM DRNGLL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382127 Genomic DNA. Translation: CAG84262.1.
RefSeq	XP_500324.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2906352.
KEGG	yli:YALI0A21263g.
Phylogenomic databases
HOGENOM	Q6CG88.
OMA	Q6CG88. DCLFSQF.
Enzyme and pathway databases
BRENDA	1.1.3.37. 3602.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALO_YARLI

Accession

Primary (citable) accession number: Q6CG88

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	August 16, 2004
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)