ARA1_YEAST
ID ARA1_YEAST Reviewed; 344 AA.
AC P38115; D6VQE4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=D-arabinose dehydrogenase [NAD(P)+] heavy chain;
DE EC=1.1.1.117;
DE AltName: Full=AKR3C;
GN Name=ARA1; OrderedLocusNames=YBR149W; ORFNames=YBR1127;
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].
RX PubMed=2005616; DOI=10.1016/0022-2836(91)90521-7;
RA Martinez-Soriano J.P., Wong W.M., van Ryk D.I., Nazar R.N.;
RT "A widely distributed 'CAT' family of repetitive DNA sequences.";
RL J. Mol. Biol. 217:629-635(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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).
RN [4]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 7-20.
RX PubMed=9920381; DOI=10.1016/s0167-4838(98)00217-9;
RA Kim S.T., Huh W.K., Lee B.H., Kang S.O.;
RT "D-arabinose dehydrogenase and its gene from Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1429:29-39(1998).
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose
CC and L-galactose in the presence of NADP(+).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose + NADP(+) = D-arabinono-1,4-lactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:21892, ChEBI:CHEBI:15378, ChEBI:CHEBI:16292,
CC ChEBI:CHEBI:46994, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.117;
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=1.1.1.117;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10.0.;
CC Temperature dependence:
CC Optimum temperature is about 30 degrees Celsius.;
CC -!- SUBUNIT: Heterodimer of a heavy chain and a light chain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 30200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; M95580; AAA35037.1; -; Genomic_DNA.
DR EMBL; Z36018; CAA85107.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07264.1; -; Genomic_DNA.
DR PIR; S46020; S46020.
DR RefSeq; NP_009707.3; NM_001178497.3.
DR PDB; 4IJC; X-ray; 2.10 A; A/B=1-344.
DR PDB; 4IJR; X-ray; 2.00 A; A/C=1-344.
DR PDBsum; 4IJC; -.
DR PDBsum; 4IJR; -.
DR AlphaFoldDB; P38115; -.
DR SMR; P38115; -.
DR BioGRID; 32848; 76.
DR DIP; DIP-4926N; -.
DR IntAct; P38115; 3.
DR MINT; P38115; -.
DR STRING; 4932.YBR149W; -.
DR iPTMnet; P38115; -.
DR MaxQB; P38115; -.
DR PaxDb; P38115; -.
DR PRIDE; P38115; -.
DR EnsemblFungi; YBR149W_mRNA; YBR149W; YBR149W.
DR GeneID; 852446; -.
DR KEGG; sce:YBR149W; -.
DR SGD; S000000353; ARA1.
DR VEuPathDB; FungiDB:YBR149W; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P38115; -.
DR OMA; AWYYGTE; -.
DR BioCyc; MetaCyc:MON-20236; -.
DR BioCyc; YEAST:MON-20236; -.
DR BRENDA; 1.1.1.117; 984.
DR BRENDA; 1.1.1.B35; 984.
DR PRO; PR:P38115; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38115; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047816; F:D-arabinose 1-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0106271; F:D-arabinose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0045290; F:D-arabinose 1-dehydrogenase [NAD(P)+] activity; IDA:SGD.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:SGD.
DR CDD; cd19119; AKR_AKR3C1; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044491; AKR3C1.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..344
FT /note="D-arabinose dehydrogenase [NAD(P)+] heavy chain"
FT /id="PRO_0000124610"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241..295
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 56..62
FT /note="AAIKAGY -> LQSKLDN (in Ref. 1; AAA35037)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..73
FT /note="YET -> SR (in Ref. 1; AAA35037)"
FT /evidence="ECO:0000305"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4IJC"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:4IJR"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4IJR"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4IJR"
SQ SEQUENCE 344 AA; 38884 MW; F9B6D9333B18FEEC CRC64;
MSSSVASTEN IVENMLHPKT TEIYFSLNNG VRIPALGLGT ANPHEKLAET KQAVKAAIKA
GYRHIDTAWA YETEPFVGEA IKELLEDGSI KREDLFITTK VWPVLWDEVD RSLNESLKAL
GLEYVDLLLQ HWPLCFEKIK DPKGISGLVK TPVDDSGKTM YAADGDYLET YKQLEKIYLD
PNDHRVRAIG VSNFSIEYLE RLIKECRVKP TVNQVETHPH LPQMELRKFC FMHDILLTAY
SPLGSHGAPN LKIPLVKKLA EKYNVTGNDL LISYHIRQGT IVIPRSLNPV RISSSIEFAS
LTKDELQELN DFGEKYPVRF IDEPFAAILP EFTGNGPNLD NLKY
