ARA2_YEAST
ID ARA2_YEAST Reviewed; 335 AA.
AC Q04212; D6VZL6; Q1XGQ6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=D-arabinose 1-dehydrogenase;
DE EC=1.1.1.116;
DE AltName: Full=NAD(+)-specific D-arabinose dehydrogenase;
GN Name=ARA2; OrderedLocusNames=YMR041C; ORFNames=YM9532.06C;
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], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17097644; DOI=10.1016/j.febslet.2006.10.058;
RA Amako K., Fujita K., Shimohata T.A., Hasegawa E., Kishimoto R., Goda K.;
RT "NAD+-specific D-arabinose dehydrogenase and its contribution to
RT erythroascorbic acid production in Saccharomyces cerevisiae.";
RL FEBS Lett. 580:6428-6434(2006).
RN [2]
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 [3]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose + NAD(+) = D-arabinono-1,4-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:20457, ChEBI:CHEBI:15378, ChEBI:CHEBI:16292,
CC ChEBI:CHEBI:46994, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.116;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.78 mM for D-arabinose {ECO:0000269|PubMed:17097644};
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; AB237161; BAE93049.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88407.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09940.1; -; Genomic_DNA.
DR PIR; S52890; S52890.
DR RefSeq; NP_013755.1; NM_001182538.1.
DR AlphaFoldDB; Q04212; -.
DR SMR; Q04212; -.
DR BioGRID; 35213; 29.
DR DIP; DIP-4506N; -.
DR IntAct; Q04212; 2.
DR MINT; Q04212; -.
DR STRING; 4932.YMR041C; -.
DR iPTMnet; Q04212; -.
DR MaxQB; Q04212; -.
DR PaxDb; Q04212; -.
DR PRIDE; Q04212; -.
DR EnsemblFungi; YMR041C_mRNA; YMR041C; YMR041C.
DR GeneID; 855057; -.
DR KEGG; sce:YMR041C; -.
DR SGD; S000004644; ARA2.
DR VEuPathDB; FungiDB:YMR041C; -.
DR eggNOG; KOG1576; Eukaryota.
DR GeneTree; ENSGT00390000005890; -.
DR HOGENOM; CLU_023205_7_2_1; -.
DR InParanoid; Q04212; -.
DR OMA; AVQSYAN; -.
DR BioCyc; MetaCyc:MON3O-32; -.
DR BioCyc; YEAST:MON3O-32; -.
DR BRENDA; 1.1.1.116; 984.
DR SABIO-RK; Q04212; -.
DR PRO; PR:Q04212; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04212; protein.
DR GO; GO:0047816; F:D-arabinose 1-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0045290; F:D-arabinose 1-dehydrogenase [NAD(P)+] activity; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosynthetic process; IMP:SGD.
DR CDD; cd19164; AKR_ARA2; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044480; Ara2-like.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR42686; PTHR42686; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..335
FT /note="D-arabinose 1-dehydrogenase"
FT /id="PRO_0000070372"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 221..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT SITE 86
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 38220 MW; CC7FA464FFAE6ED7 CRC64;
MVNEKVNPFD LASVSPLVLG GAILNQQYTD EPESIPLEDI IKYAFSHGIN AIDTSPYYGP
SEVLYGRALS NLRNEFPRDT YFICTKVGRI GAEEFNYSRD FVRFSVHRSC ERLHTTYLDL
VYLHDVEFVK FPDILEALKE LRTLKNKGVI KNFGISGYPI DFITWLAEYC STEESDIGSL
DAVLSYCNLN LQNNKLLNFR ERLLRNAKLK MVCNASILSM SLLRSQETRQ FHPCSHELRE
CASQAAKYCQ EQNVDLADLA TRYAISEWVG KGPVVLGVSS MEELKLALDN YEIVKSNGNR
LSSKDGQLVE YIQKNIFKEH FNEEWSSGIP HPEMI
