ID   ALO_CANGA               Reviewed;         525 AA.
AC   Q6FS20;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=CAGL0H04125g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380954; CAG59907.1; -; Genomic_DNA.
DR   RefSeq; XP_446974.1; XM_446974.1.
DR   AlphaFoldDB; Q6FS20; -.
DR   SMR; Q6FS20; -.
DR   STRING; 5478.XP_446974.1; -.
DR   PRIDE; Q6FS20; -.
DR   EnsemblFungi; CAG59907; CAG59907; CAGL0H04125g.
DR   GeneID; 2888523; -.
DR   KEGG; cgr:CAGL0H04125g; -.
DR   CGD; CAL0130238; CAGL0H04125g.
DR   VEuPathDB; FungiDB:CAGL0H04125g; -.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q6FS20; -.
DR   OMA; YPRFGEF; -.
DR   UniPathway; UPA00771; UER00766.
DR   Proteomes; UP000002428; Chromosome H.
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_0000128165"
FT   DOMAIN          20..195
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         58
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  59716 MW;  1EA506B8580E3E81 CRC64;
     MDLKTFGGRR NFVFRNWAGI YSSRPEWYFQ PSSVDEVVEI VKAAKLKNKT IVTVGSGHSP
     SNMCVTDEWM MNLDKMNKLL DFVENEDKTY ADVTIQGGTR LYKIHKILRE KGYAMQSLGS
     ISEQSIGGII STGTHGSSPF HGLVSSTIVN LTVVNGKGEV LFLDEKSNPE VFRAATLSLG
     KIGIIVGATV RVVPAFNIKS TQEVIKFETL LEKWDSLWTS SEFIRIWWYP YTRKCILWRG
     VKTNEPQTKS RYSWWGSTLG RFFYQTLLFI STKIYPPLTP YVERFVFRRQ YGEVETLGKG
     DVAIEDSVTG FNMDCLFSQF VDEWGCPMDN GLEVLRSLDH SIAQAAANKD FYVHVPVEVR
     CANTTLPKEQ PETSFRSNTS RGPVYGNLLR PYLDNTPSQC SYAPIHSVTN SQLTLYINAT
     IYRPFHTNAP IHKWFTLFED TMSAAGGKPH WAKNFLGSTS FAQGQVKAEG QYQDYEMRGM
     ATRVKEWYGS DLETFKKVRR EQDPDNIFLA NKQWALINGI IDENE