Reviewed, UniProtKB/Swiss-Prot Q6FS20 (ALO_CANGA)

Names and originHide

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:	CAGL0H04125g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributesHide

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)Hide

Catalytic activity	D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H2O2.
Cofactor	FAD By similarity.
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.

OntologiesHide

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)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 525	525	D-arabinono-1,4-lactone oxidase		PRO_0000128165
Regions
	Domain	20 – 195	176	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	58	1	Pros-8alpha-FAD histidine By similarity

SequencesHide

	Sequence		Length	Mass (Da)
	Q6FS20-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 1EA506B8580E3E81	FASTA	525	59,716
	10 20 30 40 50 60 MDLKTFGGRR NFVFRNWAGI YSSRPEWYFQ PSSVDEVVEI VKAAKLKNKT IVTVGSGHSP 70 80 90 100 110 120 SNMCVTDEWM MNLDKMNKLL DFVENEDKTY ADVTIQGGTR LYKIHKILRE KGYAMQSLGS 130 140 150 160 170 180 ISEQSIGGII STGTHGSSPF HGLVSSTIVN LTVVNGKGEV LFLDEKSNPE VFRAATLSLG 190 200 210 220 230 240 KIGIIVGATV RVVPAFNIKS TQEVIKFETL LEKWDSLWTS SEFIRIWWYP YTRKCILWRG 250 260 270 280 290 300 VKTNEPQTKS RYSWWGSTLG RFFYQTLLFI STKIYPPLTP YVERFVFRRQ YGEVETLGKG 310 320 330 340 350 360 DVAIEDSVTG FNMDCLFSQF VDEWGCPMDN GLEVLRSLDH SIAQAAANKD FYVHVPVEVR 370 380 390 400 410 420 CANTTLPKEQ PETSFRSNTS RGPVYGNLLR PYLDNTPSQC SYAPIHSVTN SQLTLYINAT 430 440 450 460 470 480 IYRPFHTNAP IHKWFTLFED TMSAAGGKPH WAKNFLGSTS FAQGQVKAEG QYQDYEMRGM 490 500 510 520 ATRVKEWYGS DLETFKKVRR EQDPDNIFLA NKQWALINGI IDENE

ReferencesHide

[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: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	CR380954 Genomic DNA. Translation: CAG59907.1.
RefSeq	XP_446974.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FS20.
Genome annotation databases
GeneID	2888523.
GenomeReviews	Gene locus CAGL0H04125g in contig CR380954_GR.
KEGG	cgr:CAGL0H04125g.
Phylogenomic databases
eggNOG	fuNOG04297.
HOGENOM	HBG323831.
OMA	DCLFSQF.
OrthoDB	EOG91ZGT8.
PhylomeDB	Q6FS20.
Enzyme and pathway databases
BRENDA	1.1.3.37. 189220.
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]
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 informationHide

Entry name

ALO_CANGA

Accession

Primary (citable) accession number: Q6FS20

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	July 19, 2004
Last modified:	March 23, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)