Reviewed, UniProtKB/Swiss-Prot Q6BZA0 (ALO_DEBHA)

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:	DEHA2A02904g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

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 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.

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 – 557	557	D-arabinono-1,4-lactone oxidase		PRO_0000128166
Regions
	Domain	26 – 209	184	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	63	1	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BZA0-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: D2AEE1175CCECE73	FASTA	557	63,709
	10 20 30 40 50 60 MRSDIPETLQ NFVSTKTVHQ TWAKTFFCKP QAIFQPRTVD EIRELVDQAR INGKTIMTVG 70 80 90 100 110 120 SGHSPSDMTM TKEWLCNLDR FNQVLKKEEF SGPTRNGEGE EVKFVDLTVQ AGCRIYELNR 130 140 150 160 170 180 YLKENELAIQ NLGSISDQSM AGVISTGTHG STQYHGLVSQ QVVSIEIMNS AGKLITCSSM 190 200 210 220 230 240 ENTQLFKAAM LSLGKIGIIT HVTLRTIPKY TIKSKQEIIK FDTLLKNWDT VWLDSEFIRV 250 260 270 280 290 300 WWFPYSGNCV CWRASKSSEP LSKPRDSWYG TWFGRKFYES LLWISVHICP HLTPLIEKFV 310 320 330 340 350 360 FKNQYGDVET LGHGDVAVQN SVEGLNMDCL FSQFVNEWST PLSSGQDVLI KLNDVIQTAR 370 380 390 400 410 420 EQNRFYVHAP IEVRCSNLTY SEKPFVDEND EPSLYPNKKW LAKRDRLSPG PIPGNNLRPY 430 440 450 460 470 480 LDNSSNLRYD GDGANVTNDQ LTLFINATMY RPFHTNVNSQ EWYQLFEDIM TNASGRPHWA 490 500 510 520 530 540 KNFIGVNGAH RTDQDLRKQL EFGGKTSYSM KGFNPILKKW FGENLVEYNK VRESMDPDNV 550 FLSGKDWAVR NGILIDV

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: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382133 Genomic DNA. Translation: CAG84421.2.
RefSeq	XP_456469.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2899772.
GenomeReviews	Gene locus DEHA2A02904g in contig CR382133_GR.
KEGG	dha:DEHA0A03377g.
Phylogenomic databases
eggNOG	fuNOG04297.
HOGENOM	HBG323831.
OMA	DCLFSQF.
OrthoDB	EOG91ZGT8.
Enzyme and pathway databases
BRENDA	1.1.3.37. 74267.
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_DEBHA

Accession

Primary (citable) accession number: Q6BZA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)