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   16-JUN-2009, entry version 36.
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 (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=4952;
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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY: D-arabinono-1,4-lactone + O(2) = dehydro-D-
CC       arabinono-1,4-lactone + H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbic acid
CC       biosynthesis; D-erythro-ascorbic acid from D-arabinose: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane (By similarity).
CC       Note=Membrane-embedded (By similarity).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
CC       oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR382127; CAG84262.1; -; Genomic_DNA.
DR   RefSeq; XP_500324.1; -.
DR   GeneID; 2906352; -.
DR   KEGG; yli:YALI0A21263g; -.
DR   HOGENOM; Q6CG88; -.
DR   OMA; Q6CG88; DCLFSQF.
DR   BRENDA; 1.1.3.37; 3602.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007173; ALO.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR010031; FAD_lactone_oxidase.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   TIGRFAMs; TIGR01678; FAD_lactone_ox; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Oxidoreductase.
FT   CHAIN         1    526       D-arabinono-1,4-lactone oxidase.
FT                                /FTId=PRO_0000128170.
FT   DOMAIN       22    196       FAD-binding PCMH-type.
FT   MOD_RES      59     59       Tele-8alpha-FAD histidine (By
FT                                similarity).
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
//