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P38115

- ARA1_YEAST

UniProt

P38115 - ARA1_YEAST

Protein

D-arabinose dehydrogenase [NAD(P)+] heavy chain

Gene

ARA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP+.

    Catalytic activityi

    D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H.

    pH dependencei

    Optimum pH is 10.0.

    Temperature dependencei

    Optimum temperature is about 30 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711Proton donorBy similarity
    Sitei100 – 1001Lowers pKa of active site TyrBy similarity
    Binding sitei131 – 1311SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi241 – 29555NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. alditol:NADP+ 1-oxidoreductase activity Source: SGD
    2. D-arabinose 1-dehydrogenase [NAD(P)+] activity Source: SGD

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-32366.
    MetaCyc:MONOMER3O-32367.
    YEAST:MONOMER3O-32366.
    YEAST:MONOMER3O-32367.
    ReactomeiREACT_189323. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_94166. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-arabinose dehydrogenase [NAD(P)+] heavy chain (EC:1.1.1.117)
    Alternative name(s):
    AKR3C
    Gene namesi
    Name:ARA1
    Ordered Locus Names:YBR149W
    ORF Names:YBR1127
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR149w.
    SGDiS000000353. ARA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 344344D-arabinose dehydrogenase [NAD(P)+] heavy chainPRO_0000124610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei151 – 1511Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38115.
    PaxDbiP38115.
    PeptideAtlasiP38115.

    Expressioni

    Gene expression databases

    GenevestigatoriP38115.

    Interactioni

    Subunit structurei

    Heterodimer of a heavy chain and a light chain.

    Protein-protein interaction databases

    BioGridi32848. 21 interactions.
    DIPiDIP-4926N.
    MINTiMINT-521486.
    STRINGi4932.YBR149W.

    Structurei

    Secondary structure

    1
    344
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 223
    Beta strandi23 – 264
    Beta strandi32 – 365
    Helixi44 – 496
    Helixi50 – 5910
    Beta strandi64 – 663
    Helixi69 – 713
    Helixi74 – 8613
    Helixi92 – 943
    Beta strandi96 – 1016
    Helixi103 – 1053
    Helixi109 – 12012
    Beta strandi126 – 1305
    Helixi167 – 17913
    Beta strandi185 – 1873
    Beta strandi189 – 1935
    Helixi196 – 20510
    Beta strandi211 – 2166
    Helixi224 – 23310
    Beta strandi236 – 2416
    Helixi249 – 2524
    Helixi254 – 2629
    Helixi267 – 27711
    Helixi289 – 2946
    Helixi303 – 31513
    Helixi324 – 3263
    Helixi339 – 3413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IJCX-ray2.10A/B1-344[»]
    4IJRX-ray2.00A/C1-344[»]
    ProteinModelPortaliP38115.
    SMRiP38115. Positions 15-342.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00750000117803.
    HOGENOMiHOG000250272.
    KOiK00063.
    OrthoDBiEOG7WQ83S.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38115-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSVASTEN IVENMLHPKT TEIYFSLNNG VRIPALGLGT ANPHEKLAET    50
    KQAVKAAIKA GYRHIDTAWA YETEPFVGEA IKELLEDGSI KREDLFITTK 100
    VWPVLWDEVD RSLNESLKAL GLEYVDLLLQ HWPLCFEKIK DPKGISGLVK 150
    TPVDDSGKTM YAADGDYLET YKQLEKIYLD PNDHRVRAIG VSNFSIEYLE 200
    RLIKECRVKP TVNQVETHPH LPQMELRKFC FMHDILLTAY SPLGSHGAPN 250
    LKIPLVKKLA EKYNVTGNDL LISYHIRQGT IVIPRSLNPV RISSSIEFAS 300
    LTKDELQELN DFGEKYPVRF IDEPFAAILP EFTGNGPNLD NLKY 344
    Length:344
    Mass (Da):38,884
    Last modified:October 1, 1994 - v1
    Checksum:iF9B6D9333B18FEEC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 627AAIKAGY → LQSKLDN in AAA35037. (PubMed:2005616)Curated
    Sequence conflicti71 – 733YET → SR in AAA35037. (PubMed:2005616)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95580 Genomic DNA. Translation: AAA35037.1.
    Z36018 Genomic DNA. Translation: CAA85107.1.
    BK006936 Genomic DNA. Translation: DAA07264.1.
    PIRiS46020.
    RefSeqiNP_009707.3. NM_001178497.3.

    Genome annotation databases

    EnsemblFungiiYBR149W; YBR149W; YBR149W.
    GeneIDi852446.
    KEGGisce:YBR149W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95580 Genomic DNA. Translation: AAA35037.1 .
    Z36018 Genomic DNA. Translation: CAA85107.1 .
    BK006936 Genomic DNA. Translation: DAA07264.1 .
    PIRi S46020.
    RefSeqi NP_009707.3. NM_001178497.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IJC X-ray 2.10 A/B 1-344 [» ]
    4IJR X-ray 2.00 A/C 1-344 [» ]
    ProteinModelPortali P38115.
    SMRi P38115. Positions 15-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32848. 21 interactions.
    DIPi DIP-4926N.
    MINTi MINT-521486.
    STRINGi 4932.YBR149W.

    Proteomic databases

    MaxQBi P38115.
    PaxDbi P38115.
    PeptideAtlasi P38115.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR149W ; YBR149W ; YBR149W .
    GeneIDi 852446.
    KEGGi sce:YBR149W.

    Organism-specific databases

    CYGDi YBR149w.
    SGDi S000000353. ARA1.

    Phylogenomic databases

    eggNOGi COG0656.
    GeneTreei ENSGT00750000117803.
    HOGENOMi HOG000250272.
    KOi K00063.
    OrthoDBi EOG7WQ83S.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER3O-32366.
    MetaCyc:MONOMER3O-32367.
    YEAST:MONOMER3O-32366.
    YEAST:MONOMER3O-32367.
    Reactomei REACT_189323. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_94166. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.

    Miscellaneous databases

    NextBioi 971354.

    Gene expression databases

    Genevestigatori P38115.

    Family and domain databases

    Gene3Di 3.20.20.100. 1 hit.
    InterProi IPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view ]
    PANTHERi PTHR11732. PTHR11732. 1 hit.
    Pfami PF00248. Aldo_ket_red. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000097. AKR. 1 hit.
    PRINTSi PR00069. ALDKETRDTASE.
    SUPFAMi SSF51430. SSF51430. 1 hit.
    PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A widely distributed 'CAT' family of repetitive DNA sequences."
      Martinez-Soriano J.P., Wong W.M., van Ryk D.I., Nazar R.N.
      J. Mol. Biol. 217:629-635(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "D-arabinose dehydrogenase and its gene from Saccharomyces cerevisiae."
      Kim S.T., Huh W.K., Lee B.H., Kang S.O.
      Biochim. Biophys. Acta 1429:29-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 7-20.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiARA1_YEAST
    AccessioniPrimary (citable) accession number: P38115
    Secondary accession number(s): D6VQE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 30200 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3