ALO1_CANAL
ID ALO1_CANAL Reviewed; 557 AA.
AC O93852; A0A1D8PU25; Q5ACU1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=D-arabinono-1,4-lactone oxidase {ECO:0000303|PubMed:11349062};
DE Short=ALO {ECO:0000303|PubMed:11349062};
DE EC=1.1.3.37 {ECO:0000269|PubMed:7957197};
DE EC=1.1.3.8 {ECO:0000269|PubMed:7957197};
DE EC=1.3.3.12 {ECO:0000269|PubMed:7957197};
DE AltName: Full=FAD-linked oxidoreductase ALO1 {ECO:0000305};
DE AltName: Full=L-galactono-gamma-lactone oxidase {ECO:0000303|PubMed:11349062};
GN Name=ALO1 {ECO:0000303|PubMed:11349062};
GN Synonyms=ALO {ECO:0000303|PubMed:11349062};
GN OrderedLocusNames=CAALFM_CR09790WA; ORFNames=CaO19.7551;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594;
RX PubMed=11349062; DOI=10.1128/iai.69.6.3939-3946.2001;
RA Huh W.-K., Kim S.-T., Kim H., Jeong G., Kang S.-O.;
RT "Deficiency of D-erythroascorbic acid attenuates hyphal growth and
RT virulence of Candida albicans.";
RL Infect. Immun. 69:3939-3946(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=7957197; DOI=10.1111/j.1432-1033.1994.1073b.x;
RA Huh W.K., Kim S.T., Yang K.S., Seok Y.J., Hah Y.C., Kang S.O.;
RT "Characterisation of D-arabinono-1,4-lactone oxidase from Candida albicans
RT ATCC 10231.";
RL Eur. J. Biochem. 225:1073-1079(1994).
CC -!- FUNCTION: D-arabinono-1,4-lactone oxidase that catalyzes the final step
CC of biosynthesis of D-erythroascorbic acid, an important antioxidant and
CC one of the virulence factors enhancing the pathogenicity
CC (PubMed:11349062, PubMed:7957197). Is also able to oxidize L-galactono-
CC 1,4-lactone, L-xylono-1,4-lactone and L-gulono-1,4-lactone
CC (PubMed:7957197). {ECO:0000269|PubMed:11349062,
CC ECO:0000269|PubMed:7957197}.
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:7957197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23757;
CC Evidence={ECO:0000269|PubMed:7957197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-galactono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC Xref=Rhea:RHEA:20617, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17464, ChEBI:CHEBI:38290; EC=1.3.3.12;
CC Evidence={ECO:0000269|PubMed:7957197};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20619;
CC Evidence={ECO:0000269|PubMed:7957197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8;
CC Evidence={ECO:0000269|PubMed:7957197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32364;
CC Evidence={ECO:0000269|PubMed:7957197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-xylono-1,4-lactone + O2 = dehydro-L-arabinono-1,4-lactone +
CC H(+) + H2O2; Xref=Rhea:RHEA:68360, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18118,
CC ChEBI:CHEBI:177361; Evidence={ECO:0000269|PubMed:7957197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68361;
CC Evidence={ECO:0000269|PubMed:7957197};
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:0000269|PubMed:7957197}.
CC -!- DISRUPTION PHENOTYPE: Abolishes D-arabinono-1,4-lactone oxidase
CC activity and impairs the production of D-erythroascorbic acid
CC (PubMed:11349062). Leads to increased sensitivity towards oxidative
CC stress, defective hyphal growth and attenuated virulence
CC (PubMed:11349062). {ECO:0000269|PubMed:11349062}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF031228; AAC98913.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31636.1; -; Genomic_DNA.
DR RefSeq; XP_719313.1; XM_714220.1.
DR AlphaFoldDB; O93852; -.
DR SMR; O93852; -.
DR BioGRID; 1222077; 1.
DR STRING; 237561.O93852; -.
DR PRIDE; O93852; -.
DR GeneID; 3638983; -.
DR KEGG; cal:CAALFM_CR09790WA; -.
DR CGD; CAL0000174500; ALO1.
DR VEuPathDB; FungiDB:CR_09790W_A; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; O93852; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 1134169at2759; -.
DR UniPathway; UPA00771; UER00766.
DR PHI-base; PHI:197; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IDA:CGD.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050024; F:L-galactonolactone oxidase activity; IEA:RHEA.
DR GO; GO:0050105; F:L-gulonolactone oxidase activity; IEA:RHEA.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006767; P:water-soluble vitamin metabolic process; IC:CGD.
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 FAD; Flavoprotein; Oxidoreductase; Reference proteome; Virulence.
FT CHAIN 1..557
FT /note="D-arabinono-1,4-lactone oxidase"
FT /id="PRO_0000128164"
FT DOMAIN 25..209
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 58..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 62..63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 144..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 199
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT BINDING 543..546
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9FUJ1"
FT MOD_RES 62
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 557 AA; 63447 MW; 0348233954111D92 CRC64;
MTDIPESLKP FVTKKVIHST WAGTFLCKPQ AIFQPRNVEE IQELIKQARL HGKTIMTVGS
GHSPSDLTMT TEWLCNLDKF NHVLLEEPYY APKSPTDDTP EIKFVDLTVE AGTRIFELNE
YLKRNNLAIQ NLGSISDQSI AGLISTGTHG STQYHGLVSQ QVVSVKFLNS AGELITCSSV
DKPEYFRAIL LSLGKIGIIT HVTLRTCPKY TIKSKQEIIN FETLLNNWDN LWLESEFIRI
WWFPYTNKCV LWRANKSTDP LSDPRPSWYG TKLGRFFYES LLWVSVHLFP RLTPFVEKFV
FGQQYGEVET LGKGDIAVQN SVEGLNMDCL FSQFVNEWSS PLNSGPEILT ELKKIITDAS
QTGDFFVHAP IEVRCSNVTY SDEPFTDDKN QKSLYPSQEW LSNRSKTSAG PIPGNNLRPY
LDNSPKLPYS KDGKITNDQL TLFINATMYR PFGTNVETHK WFQLFEDVMS KAGGKPHWAK
NFIGLTQDEK YDKQQDLKTQ LEFGGKPFYT MLGFKPVMQD WFGKDLVAFN KVRKETDPDG
VFLSGKVWAE RNGILLD
