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   27-MAR-2024, entry version 137.
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; 284812.Q9HDX8; -.
DR   iPTMnet; Q9HDX8; -.
DR   MaxQB; Q9HDX8; -.
DR   PaxDb; 4896-SPAPB1A10-12c-1; -.
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:0005741; C: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; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; ISO:PomBase.
DR   GO; GO:0006766; P:vitamin metabolic process; IC:PomBase.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2520; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR030654; Sugar_lactone_oxidase.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   NCBIfam; TIGR01678; FAD_lactone_ox; 1.
DR   PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PIRSF; PIRSF000136; LGO_GLO; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 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
//