ID   ALO_YARLI               Reviewed;         526 AA.
AC   Q6CG88;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=YALI0A21263g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382127; CAG84262.1; -; Genomic_DNA.
DR   RefSeq; XP_500324.1; XM_500324.1.
DR   AlphaFoldDB; Q6CG88; -.
DR   SMR; Q6CG88; -.
DR   STRING; 284591.Q6CG88; -.
DR   EnsemblFungi; CAG84262; CAG84262; YALI0_A21263g.
DR   GeneID; 2906352; -.
DR   KEGG; yli:YALI0A21263g; -.
DR   VEuPathDB; FungiDB:YALI0_A21263g; -.
DR   HOGENOM; CLU_003896_4_1_1; -.
DR   InParanoid; Q6CG88; -.
DR   OMA; YPRFGEF; -.
DR   OrthoDB; 53654at2759; -.
DR   UniPathway; UPA00771; UER00766.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:EnsemblFungi.
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: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; 3.30.465.10; -; 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   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..526
FT                   /note="D-arabinono-1,4-lactone oxidase"
FT                   /id="PRO_0000128170"
FT   DOMAIN          22..196
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         59
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  58900 MW;  19AC25D2944948A1 CRC64;
     MSLRNSTTAK RFHSHKTWAG TFWSRPSLYF QPASIEELQA IVTRARDLGK TIMVVGSAHS
     PSDLTMTSQW LVNLDKLSKA VSFKPHTSGL YTDVTVEAGI RIHQLNEVLK RKGLAMQNLG
     SISDQSVAGI ISTGTHGSSA YHGLVSQQIV SLTIMIASGE LLTCSPDENP TLFRAALLSL
     GKLGIIVYAT LRTVPAYTIH STQHVITFET LIREWDNLWT ASEYIRVWWF PYAERCILWR
     ASKSELPLSA PRPSWYGTWL GRLFYETLLW VSVRLWPSLT PSVERFIFSR QYGMEDTLGS
     GTGSEAVQGS VEGLNMDCLF SQFVNEWGMP LDNGPDVLRA LRAKIEAAAK DNIYYVHSPV
     EVRCSNMSVP DSGDRNVEPN TQEFSASRRG AITGNTLRPL LDINPRDRPY ASPHGHVTNS
     NLTLYINATM YRPFGVNSPV GKWYRDFEGI VAEAGGKPHW AKNFLGPETA ELKDNESEDG
     KMLGLKPIID EWYGDDLKQW KSLREKYDPT GVFLSGKVWM DRNGLL
//