Reviewed, UniProtKB/Swiss-Prot Q9HDX8 (ALO_SCHPO)

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
ORF Names:	SPAPB1A10.12c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2).
Cofactor	FAD By similarity.
Pathway	Cofactor biosynthesis; D-erythroascorbic acid biosynthesis; D-erythro-ascorbic acid from D-arabinose: step 2/2.
Subcellular location	Mitochondrion membraneBy 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	cellular response to oxidative stress Inferred from expression pattern. Source: GeneDB_SPombe
Cellular component	mitochondrion Inferred from direct assay. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	D-arabinono-1,4-lactone oxidase		PRO_0000128169
Regions
	Domain	24 – 194	171	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	61	1	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDX8-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: A3BE6D8D08E2F273	FASTA	461	52,028
	10 20 30 40 50 60 MSIPHINKLS QDGRVRFSNW AKTFSAISLG LRCPKTEEQL REILVDANSN GKKIRVVGAG 70 80 90 100 110 120 HSPSDIVCTS GYLLSLDKMN KVVSFDPDSL SITVQAGIRF YQVQEILQNL GYSLPIVGSI 130 140 150 160 170 180 SETSVSGIMS TCTHGSSLQH QVLPHYIKSM RIMLADGSIV TCSRELQKDM FAAAQVSLGA 190 200 210 220 230 240 LGVIVDITIS VVPAFDLVAT EDVTTVTDLF QDWKNNLIWE SAEFVRVHVF PYANRAVVWR 250 260 270 280 290 300 ANKVEPNTVP HTPKPSLFRL KLDSFVYQCL LFVGKCVNRV TPYLERFWFK CHYGSKLGTA 310 320 330 340 350 360 LQVAGPGFDV LQMFCYFSQH VSEWGIPLES APDALEKLIN YTVDDAGKIG AYTHWPIEVR 370 380 390 400 410 420 VCAPTPEDEC WLSTDCKVPT CYIEAIMYRP FSTSINYKPY FKALEDIANQ YNGKPHWAKE 430 440 450 460 YSLTKEQLLE RYPNLSKWLS LRKLLDPKGV FWNDYLQRHL G

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAC21485.1.
RefSeq	NP_593526.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2543430.
KEGG	spo:SPAPB1A10.12c.
NMPDR	fig|4896.1.peg.3496.
Organism-specific databases
GeneDB_Spombe	SPAPB1A10.12c.
Gene expression databases
ArrayExpress	Q9HDX8.
Family and domain databases
InterPro	IPR007173. ALO. 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]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

ALO_SCHPO

Accession

Primary (citable) accession number: Q9HDX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	March 1, 2001
Last modified:	November 4, 2008
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)