Reviewed, UniProtKB/Swiss-Prot Q6CSY3 (ALO_KLULA)

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:	KLLA0C16896g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

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_0000128167
Regions
	Domain	23 – 197	175	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	60	1	Pros-8alpha-FAD histidine By similarity

SequencesHide

	Sequence		Length	Mass (Da)
	Q6CSY3-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 2C3487B581F808E6	FASTA	525	59,206
	10 20 30 40 50 60 MSFDLVAGNA RSNFVFKNWA GIYSCRPQLY FQPNSIDEVV QIVKAAIEQG KTIVTVGSGH 70 80 90 100 110 120 SPSDMCVTDQ WLMNLDNLNS VVEFKENKEE LYADVTVEAG LRIYQLSEIL AEKGYAIQNL 130 140 150 160 170 180 GSISEQSVAG IISTGTHGSS PYHGLVSSQY VNLTIVNGKG EVVFLDSENS PEVFRAATLS 190 200 210 220 230 240 LGKIGIIVKA TIRVIPEFNI KSTQEVIHFE TLLNNWETIW TSSEFIRCWW YPYTRKVVLW 250 260 270 280 290 300 RGSKTEEPLT APRKSWWGST FGRFIYESLI WISVKIYPAL TPYVESFVFH QQYGRVETYG 310 320 330 340 350 360 SGDVSVQTSI AGLNMDCLFS QFVDEWGCPL NNGPEVLRSL DYSITQAAQN KEFFVHVPVE 370 380 390 400 410 420 VRCSNTTLPA EIPDYSNRTK TSAGPVFGNT LRPYLDATPR HLRYAPLSDV TNSQLSLYIN 430 440 450 460 470 480 ATIYRPFGSN SPIHKWFTLF EDTMGAAGGK PHWAKNFLGA TSMAAGKVKD EKDYDDYEMR 490 500 510 520 GMATKIKEWY GEDLLKFREI RSQQDPNNVF MANKEWAIRN GIIEP

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 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	CR382123 Genomic DNA. Translation: CAH01807.1.
RefSeq	XP_452956.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CSY3.
Genome annotation databases
GeneID	2892284.
GenomeReviews	Gene locus KLLA0C16896g in contig CR382123_GR.
KEGG	kla:KLLA0C16896g.
Phylogenomic databases
eggNOG	fuNOG04297.
HOGENOM	HBG323831.
OMA	DCLFSQF.
OrthoDB	EOG91ZGT8.
PhylomeDB	Q6CSY3.
Enzyme and pathway databases
BRENDA	1.1.3.37. 74088.
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_KLULA

Accession

Primary (citable) accession number: Q6CSY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	August 16, 2004
Last modified:	March 23, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)