ALO_YEAST
ID ALO_YEAST Reviewed; 526 AA.
AC P54783; D6W0J7; O42618;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=D-arabinono-1,4-lactone oxidase;
DE Short=ALO;
DE EC=1.1.3.37 {ECO:0000269|PubMed:10094636};
DE AltName: Full=L-galactono-gamma-lactone oxidase;
GN Name=ALO1; OrderedLocusNames=YML086C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 86-105 AND 349-363,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 44774 / DBY747;
RX PubMed=10094636; DOI=10.1046/j.1365-2958.1998.01133.x;
RA Huh W.-K., Lee B.-H., Kim S.-T., Kim Y.-R., Rhie G.-E., Baek Y.-W.,
RA Hwang C.-S., Lee J.-S., Kang S.-O.;
RT "D-erythroascorbic acid is an important antioxidant molecule in
RT Saccharomyces cerevisiae.";
RL Mol. Microbiol. 30:895-903(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nishikimi M., Ohata Y., Ishikawa T.;
RT "Identification of the yeast genomic sequence encoding L-galactono-gamma-
RT lactone oxidase.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Can oxidize L-gulono-1,4-lactone as well as D-arabinono-1,4-
CC lactone and L-galactono-1,4-lactone. {ECO:0000269|PubMed:10094636}.
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 Evidence={ECO:0000269|PubMed:10094636};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbate biosynthesis;
CC dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2.
CC {ECO:0000305|PubMed:10094636}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10094636}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane. Note=Membrane-embedded.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 6190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; U40390; AAC98538.1; -; Genomic_DNA.
DR EMBL; AB009401; BAA23804.1; -; Genomic_DNA.
DR EMBL; Z46660; CAA86652.1; -; Genomic_DNA.
DR EMBL; AY693120; AAT93139.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09811.1; -; Genomic_DNA.
DR PIR; S49641; S49641.
DR RefSeq; NP_013624.1; NM_001182445.1.
DR AlphaFoldDB; P54783; -.
DR SMR; P54783; -.
DR BioGRID; 35055; 130.
DR IntAct; P54783; 40.
DR MINT; P54783; -.
DR STRING; 4932.YML086C; -.
DR iPTMnet; P54783; -.
DR MaxQB; P54783; -.
DR PaxDb; P54783; -.
DR PRIDE; P54783; -.
DR DNASU; 854888; -.
DR EnsemblFungi; YML086C_mRNA; YML086C; YML086C.
DR GeneID; 854888; -.
DR KEGG; sce:YML086C; -.
DR SGD; S000004551; ALO1.
DR VEuPathDB; FungiDB:YML086C; -.
DR eggNOG; KOG4730; Eukaryota.
DR GeneTree; ENSGT00510000049722; -.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; P54783; -.
DR OMA; YPRFGEF; -.
DR BioCyc; MetaCyc:YML086C-MON; -.
DR BioCyc; YEAST:YML086C-MON; -.
DR BRENDA; 1.1.3.37; 984.
DR UniPathway; UPA00771; UER00766.
DR PRO; PR:P54783; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P54783; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IDA:SGD.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..526
FT /note="D-arabinono-1,4-lactone oxidase"
FT /id="PRO_0000128171"
FT DOMAIN 19..193
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 56
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CONFLICT 417
FT /note="A -> P (in Ref. 2; BAA23804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59494 MW; 942177A74A738EC8 CRC64;
MSTIPFRKNY VFKNWAGIYS AKPERYFQPS SIDEVVELVK SARLAEKSLV TVGSGHSPSN
MCVTDEWLVN LDRLDKVQKF VEYPELHYAD VTVDAGMRLY QLNEFLGAKG YSIQNLGSIS
EQSVAGIIST GSHGSSPYHG LISSQYVNLT IVNGKGELKF LDAENDPEVF KAALLSVGKI
GIIVSATIRV VPGFNIKSTQ EVITFENLLK QWDTLWTSSE FIRVWWYPYT RKCVLWRGNK
TTDAQNGPAK SWWGTKLGRF FYETLLWIST KIYAPLTPFV EKFVFNRQYG KLEKSSTGDV
NVTDSISGFN MDCLFSQFVD EWGCPMDNGL EVLRSLDHSI AQAAINKEFY VHVPMEVRCS
NTTLPSEPLD TSKRTNTSPG PVYGNVCRPF LDNTPSHCRF APLENVTNSQ LTLYINATIY
RPFGCNTPIH KWFTLFENTM MVAGGKPHWA KNFLGSTTLA AGPVKKDTDY DDFEMRGMAL
KVEEWYGEDL KKFRKIRKEQ DPDNVFLANK QWAIINGIID PSELSD
