ID   ALO_ASHGO               Reviewed;         532 AA.
AC   Q752Y3;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
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=AFR440C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53811.1; -; Genomic_DNA.
DR   RefSeq; NP_985987.1; NM_211342.1.
DR   AlphaFoldDB; Q752Y3; -.
DR   SMR; Q752Y3; -.
DR   STRING; 33169.AAS53811; -.
DR   PRIDE; Q752Y3; -.
DR   EnsemblFungi; AAS53811; AAS53811; AGOS_AFR440C.
DR   GeneID; 4622264; -.
DR   KEGG; ago:AGOS_AFR440C; -.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q752Y3; -.
DR   OMA; YPRFGEF; -.
DR   UniPathway; UPA00771; UER00766.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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..532
FT                   /note="D-arabinono-1,4-lactone oxidase"
FT                   /id="PRO_0000128163"
FT   DOMAIN          25..199
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         62
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  59965 MW;  8B975E346283331C CRC64;
     MSVLAGVEAS GIARNYVFKN WAGIYSARPR LYFQPRSEDE VVAIVRAARE QGRTIVTVGS
     GHSPSDMCAT DDWMVNLDRL NGVLELQEDE QGRYADVTVA AGIRVYELHR YLSARGYALQ
     NLGSISEQSV GGIISTGTHG SSPYHGLVSS QYVNLTLVNG RGELVFLDSE HEPEVFRAAM
     LSLGKLGIIV RATIRVVPAF NIHSTQEVIN FETLLDNWET IWTSSEFIRC WWYPYVRKCV
     LWRGVKTSEP AEKSRSSWWG TTLGRLVYES LLWLTVNVYP SLTPFVERFI FRQQYGKVET
     FGNGDEAVQT SIDGLNMDCL FSQFVDEWAC PLNNGPEVLR SLDHSIAQAA QNKEFFVHVP
     IEVRCSNTTL PHEYKCPEDR TVTAPGPVYG NLLRPYLDNT PSHLRYAPLS DVTNSQLTLY
     INATIYRPFG TNTPIHKWFT LFEDTLGAAG GKPHWAKNFL GSTATAAGPV KSSDEYQDYE
     MRGMATKIKE WYGDNLKQFQ KVRREQDPHN VFIANKDWAV KNGIIDIDEL DS