ALO_SCHPO
ID ALO_SCHPO Reviewed; 461 AA.
AC Q9HDX8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=D-arabinono-1,4-lactone oxidase;
DE Short=ALO;
DE EC=1.1.3.37;
DE AltName: Full=L-galactono-gamma-lactone oxidase;
GN Name=alo1; ORFNames=SPAPB1A10.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone
CC + H(+) + H2O2; Xref=Rhea:RHEA:23756, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16292,
CC ChEBI:CHEBI:58277; EC=1.1.3.37;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbate biosynthesis;
CC dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
CC Note=Membrane-embedded. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAC21485.1; -; Genomic_DNA.
DR RefSeq; NP_593526.1; NM_001018960.2.
DR AlphaFoldDB; Q9HDX8; -.
DR SMR; Q9HDX8; -.
DR BioGRID; 279850; 4.
DR STRING; 4896.SPAPB1A10.12c.1; -.
DR MaxQB; Q9HDX8; -.
DR PaxDb; Q9HDX8; -.
DR PRIDE; Q9HDX8; -.
DR EnsemblFungi; SPAPB1A10.12c.1; SPAPB1A10.12c.1:pep; SPAPB1A10.12c.
DR GeneID; 2543430; -.
DR KEGG; spo:SPAPB1A10.12c; -.
DR PomBase; SPAPB1A10.12c; alo1.
DR VEuPathDB; FungiDB:SPAPB1A10.12c; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; Q9HDX8; -.
DR OMA; YPRFGEF; -.
DR PhylomeDB; Q9HDX8; -.
DR UniPathway; UPA00771; UER00766.
DR PRO; PR:Q9HDX8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; ISO:PomBase.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; ISO:PomBase.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR030654; Sugar_lactone_oxidase.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; PTHR43762; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR01678; FAD_lactone_ox; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..461
FT /note="D-arabinono-1,4-lactone oxidase"
FT /id="PRO_0000128169"
FT DOMAIN 24..194
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 61
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 461 AA; 52028 MW; A3BE6D8D08E2F273 CRC64;
MSIPHINKLS QDGRVRFSNW AKTFSAISLG LRCPKTEEQL REILVDANSN GKKIRVVGAG
HSPSDIVCTS GYLLSLDKMN KVVSFDPDSL SITVQAGIRF YQVQEILQNL GYSLPIVGSI
SETSVSGIMS TCTHGSSLQH QVLPHYIKSM RIMLADGSIV TCSRELQKDM FAAAQVSLGA
LGVIVDITIS VVPAFDLVAT EDVTTVTDLF QDWKNNLIWE SAEFVRVHVF PYANRAVVWR
ANKVEPNTVP HTPKPSLFRL KLDSFVYQCL LFVGKCVNRV TPYLERFWFK CHYGSKLGTA
LQVAGPGFDV LQMFCYFSQH VSEWGIPLES APDALEKLIN YTVDDAGKIG AYTHWPIEVR
VCAPTPEDEC WLSTDCKVPT CYIEAIMYRP FSTSINYKPY FKALEDIANQ YNGKPHWAKE
YSLTKEQLLE RYPNLSKWLS LRKLLDPKGV FWNDYLQRHL G
