Q9HDX8 (ALO_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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 (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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 Reference proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro cellular response to oxidative stress Inferred from expression pattern. Source: GeneDB_Spombe
Cellular component	integral to mitochondrial outer membrane Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Molecular function	D-arabinono-1,4-lactone oxidase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide 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 – 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	Pros-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDX8 [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: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC21485.1.
RefSeq	NP_593526.1. NM_001018960.1.
3D structure databases
ProteinModelPortal	Q9HDX8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAPB1A10.12c.1; SPAPB1A10.12c.1:pep; SPAPB1A10.12c.
GeneID	2543430.
GenomeReviews	Gene locus alo1 in contig CU329670_GR.
KEGG	spo:SPAPB1A10.12c.
NMPDR	fig|4896.1.peg.3496.
Organism-specific databases
GeneDB_Spombe	SPAPB1A10.12c.
Phylogenomic databases
eggNOG	fuNOG04297.
GeneTree	EFGT00050000001279.
HOGENOM	HBG323831.
OMA	DCLFSQF.
OrthoDB	EOG4GF6PD.
Gene expression databases
ArrayExpress	Q9HDX8.
Family and domain databases
InterPro	IPR007173. ALO. IPR016166. FAD-bd_2. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR010031. FAD_lactone_oxidase. IPR023595. LGO_GLO. IPR006094. Oxid_FAD_bind_N. [Graphical view]
Gene3D	G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
Pfam	PF04030. ALO. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
PIRSF	PIRSF000136. LGO_GLO. 1 hit.
SUPFAM	SSF56176. FAD-binding_2. 1 hit.
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_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:	December 14, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program