ID   ALO_DEBHA               Reviewed;         557 AA.
AC   Q6BZA0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=DEHA2A02904g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84421.2; -; Genomic_DNA.
DR   RefSeq; XP_456469.2; XM_456469.1.
DR   AlphaFoldDB; Q6BZA0; -.
DR   STRING; 4959.XP_456469.2; -.
DR   EnsemblFungi; CAG84421; CAG84421; DEHA2A02904g.
DR   GeneID; 2899772; -.
DR   KEGG; dha:DEHA2A02904g; -.
DR   VEuPathDB; FungiDB:DEHA2A02904g; -.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q6BZA0; -.
DR   OMA; YPRFGEF; -.
DR   OrthoDB; 1134169at2759; -.
DR   UniPathway; UPA00771; UER00766.
DR   Proteomes; UP000000599; Chromosome A.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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   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..557
FT                   /note="D-arabinono-1,4-lactone oxidase"
FT                   /id="PRO_0000128166"
FT   DOMAIN          26..209
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         63
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  63709 MW;  D2AEE1175CCECE73 CRC64;
     MRSDIPETLQ NFVSTKTVHQ TWAKTFFCKP QAIFQPRTVD EIRELVDQAR INGKTIMTVG
     SGHSPSDMTM TKEWLCNLDR FNQVLKKEEF SGPTRNGEGE EVKFVDLTVQ AGCRIYELNR
     YLKENELAIQ NLGSISDQSM AGVISTGTHG STQYHGLVSQ QVVSIEIMNS AGKLITCSSM
     ENTQLFKAAM LSLGKIGIIT HVTLRTIPKY TIKSKQEIIK FDTLLKNWDT VWLDSEFIRV
     WWFPYSGNCV CWRASKSSEP LSKPRDSWYG TWFGRKFYES LLWISVHICP HLTPLIEKFV
     FKNQYGDVET LGHGDVAVQN SVEGLNMDCL FSQFVNEWST PLSSGQDVLI KLNDVIQTAR
     EQNRFYVHAP IEVRCSNLTY SEKPFVDEND EPSLYPNKKW LAKRDRLSPG PIPGNNLRPY
     LDNSSNLRYD GDGANVTNDQ LTLFINATMY RPFHTNVNSQ EWYQLFEDIM TNASGRPHWA
     KNFIGVNGAH RTDQDLRKQL EFGGKTSYSM KGFNPILKKW FGENLVEYNK VRESMDPDNV
     FLSGKDWAVR NGILIDV