Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADPH-dependent alpha-keto amide reductase

Gene

YDL124W

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reduces aromatic alpha-keto amides, aliphatic and aromatic alpha-keto esters, but not beta-keto esters.1 Publication

Kineticsi

  1. KM=146 µM for o-chlorobenzoylformamide1 Publication
  2. KM=156 µM for m-chlorobenzoylformamide1 Publication
  3. KM=231 µM for p-chlorobenzoylformamide1 Publication
  4. KM=103 µM for benzoylformamide1 Publication
  5. KM=254 µM for 3-methyl-2-oxobutanoate1 Publication

    pH dependencei

    Stable from pH 6 to 9.5.1 Publication

    Temperature dependencei

    Thermostable up to 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei64 – 641Proton donorBy similarity
    Sitei89 – 891Lowers pKa of active site TyrBy similarity
    Binding sitei122 – 1221SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi208 – 26861NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    • alditol:NADP+ 1-oxidoreductase activity Source: SGD
    • aldo-keto reductase (NADP) activity Source: SGD
    • alpha-keto amide reductase activity Source: SGD
    • alpha-keto ester reductase activity Source: SGD

    GO - Biological processi

    • cellular amide metabolic process Source: SGD
    • cellular aromatic compound metabolic process Source: SGD
    • cellular ketone metabolic process Source: SGD
    • cellular response to oxidative stress Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29523-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent alpha-keto amide reductase (EC:1.2.1.-)
    Short name:
    AKR-E
    Alternative name(s):
    YKAR
    Gene namesi
    Ordered Locus Names:YDL124W
    ORF Names:D2240
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDL124W.
    SGDiS000002282. YDL124W.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312NADPH-dependent alpha-keto amide reductasePRO_0000262755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei123 – 1231PhosphoserineCombined sources

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ07551.
    TopDownProteomicsiQ07551.

    2D gel databases

    UCD-2DPAGEQ07551.

    PTM databases

    iPTMnetiQ07551.

    Expressioni

    Inductioni

    Transiently induced shortly after the switch from aerobic to anaerobic growth (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi31939. 14 interactions.
    DIPiDIP-6607N.
    MINTiMINT-4479375.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07551.
    SMRiQ07551. Positions 22-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00830000129046.
    HOGENOMiHOG000250272.
    InParanoidiQ07551.
    OMAiEVKPQVN.
    OrthoDBiEOG7WQ83S.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    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.
    PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07551-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSFHQQFFTL NNGNKIPAIA IIGTGTRWYK NEETDATFSN SLVEQIVYAL
    60 70 80 90 100
    KLPGIIHIDA AEIYRTYPEV GKALSLTEKP RNAIFLTDKY SPQIKMSDSP
    110 120 130 140 150
    ADGLDLALKK MGTDYVDLYL LHSPFVSKEV NGLSLEEAWK DMEQLYKSGK
    160 170 180 190 200
    AKNIGVSNFA VEDLQRILKV AEVKPQVNQI EFSPFLQNQT PGIYKFCQEH
    210 220 230 240 250
    DILVEAYSPL GPLQKKTAQD DSQPFFEYVK ELSEKYIKSE AQIILRWVTK
    260 270 280 290 300
    RGVLPVTTSS KPQRISDAQN LFSFDLTAEE VDKITELGLE HEPLRLYWNK
    310
    LYGKYNYAAQ KV
    Length:312
    Mass (Da):35,561
    Last modified:November 1, 1996 - v1
    Checksum:i165ADCB5C1952AF0
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z74172 Genomic DNA. Translation: CAA98692.1.
    BK006938 Genomic DNA. Translation: DAA11736.1.
    PIRiS67667.
    RefSeqiNP_010159.1. NM_001180183.1.

    Genome annotation databases

    EnsemblFungiiYDL124W; YDL124W; YDL124W.
    GeneIDi851433.
    KEGGisce:YDL124W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z74172 Genomic DNA. Translation: CAA98692.1.
    BK006938 Genomic DNA. Translation: DAA11736.1.
    PIRiS67667.
    RefSeqiNP_010159.1. NM_001180183.1.

    3D structure databases

    ProteinModelPortaliQ07551.
    SMRiQ07551. Positions 22-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31939. 14 interactions.
    DIPiDIP-6607N.
    MINTiMINT-4479375.

    PTM databases

    iPTMnetiQ07551.

    2D gel databases

    UCD-2DPAGEQ07551.

    Proteomic databases

    MaxQBiQ07551.
    TopDownProteomicsiQ07551.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDL124W; YDL124W; YDL124W.
    GeneIDi851433.
    KEGGisce:YDL124W.

    Organism-specific databases

    EuPathDBiFungiDB:YDL124W.
    SGDiS000002282. YDL124W.

    Phylogenomic databases

    GeneTreeiENSGT00830000129046.
    HOGENOMiHOG000250272.
    InParanoidiQ07551.
    OMAiEVKPQVN.
    OrthoDBiEOG7WQ83S.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29523-MONOMER.

    Miscellaneous databases

    PROiQ07551.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    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.
    PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Purification and characterization of alpha-keto amide reductase from Saccharomyces cerevisiae."
      Ishihara K., Yamamoto H., Mitsuhashi K., Nishikawa K., Tsuboi S., Tsuji H., Nakajima N.
      Biosci. Biotechnol. Biochem. 68:2306-2312(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 265-276, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION, SUBUNIT.
    4. Cited for: FUNCTION.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Proteome analysis of recombinant xylose-fermenting Saccharomyces cerevisiae."
      Salusjaervi L., Poutanen M., Pitkaenen J.-P., Koivistoinen H., Aristidou A., Kalkkinen N., Ruohonen L., Penttilae M.
      Yeast 20:295-314(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "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 SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKAR_YEAST
    AccessioniPrimary (citable) accession number: Q07551
    Secondary accession number(s): D6VRM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 1, 1996
    Last modified: July 6, 2016
    This is version 114 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 4030 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.