ID   ALO_KLULA               Reviewed;         525 AA.
AC   Q6CSY3;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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; OrderedLocusNames=KLLA0C16896g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382123; CAH01807.1; -; Genomic_DNA.
DR   RefSeq; XP_452956.1; XM_452956.1.
DR   AlphaFoldDB; Q6CSY3; -.
DR   SMR; Q6CSY3; -.
DR   STRING; 28985.XP_452956.1; -.
DR   PRIDE; Q6CSY3; -.
DR   EnsemblFungi; CAH01807; CAH01807; KLLA0_C16896g.
DR   GeneID; 2892284; -.
DR   KEGG; kla:KLLA0_C16896g; -.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q6CSY3; -.
DR   OMA; YPRFGEF; -.
DR   UniPathway; UPA00771; UER00766.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:EnsemblFungi.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; IEA:EnsemblFungi.
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; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   InterPro; IPR030654; Sugar_lactone_oxidase.
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.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..525
FT                   /note="D-arabinono-1,4-lactone oxidase"
FT                   /id="PRO_0000128167"
FT   DOMAIN          23..197
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         60
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  59206 MW;  2C3487B581F808E6 CRC64;
     MSFDLVAGNA RSNFVFKNWA GIYSCRPQLY FQPNSIDEVV QIVKAAIEQG KTIVTVGSGH
     SPSDMCVTDQ WLMNLDNLNS VVEFKENKEE LYADVTVEAG LRIYQLSEIL AEKGYAIQNL
     GSISEQSVAG IISTGTHGSS PYHGLVSSQY VNLTIVNGKG EVVFLDSENS PEVFRAATLS
     LGKIGIIVKA TIRVIPEFNI KSTQEVIHFE TLLNNWETIW TSSEFIRCWW YPYTRKVVLW
     RGSKTEEPLT APRKSWWGST FGRFIYESLI WISVKIYPAL TPYVESFVFH QQYGRVETYG
     SGDVSVQTSI AGLNMDCLFS QFVDEWGCPL NNGPEVLRSL DYSITQAAQN KEFFVHVPVE
     VRCSNTTLPA EIPDYSNRTK TSAGPVFGNT LRPYLDATPR HLRYAPLSDV TNSQLSLYIN
     ATIYRPFGSN SPIHKWFTLF EDTMGAAGGK PHWAKNFLGA TSMAAGKVKD EKDYDDYEMR
     GMATKIKEWY GEDLLKFREI RSQQDPNNVF MANKEWAIRN GIIEP