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P37402

- PANE_SALTY

UniProt

P37402 - PANE_SALTY

Protein

2-dehydropantoate 2-reductase

Gene

panE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. Has a strong preference for NADPH over NADH as the electron acceptor. Pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvate, alpha-ketoglutarate, alpha-ketobutyrate, and acetaldehyde can not served as substrates for reduction.1 Publication

    Catalytic activityi

    (R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.1 Publication

    Kineticsi

    1. KM=0.0776 mM for NADPH1 Publication
    2. KM=0.0742 mM for 2-dehydropantoate1 Publication

    Vmax=89.3 µmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 6.25.1 Publication

    Temperature dependencei

    Optimum temperature is 42 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei31 – 311NADP; via amide nitrogenBy similarity
    Binding sitei98 – 981NADP; via amide nitrogenBy similarity
    Binding sitei98 – 981SubstrateBy similarity
    Binding sitei122 – 1221NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Active sitei176 – 1761Proton donor
    Binding sitei180 – 1801SubstrateBy similarity
    Binding sitei184 – 1841SubstrateBy similarity
    Binding sitei194 – 1941SubstrateBy similarity
    Binding sitei241 – 2411SubstrateBy similarity
    Binding sitei244 – 2441SubstrateBy similarity
    Binding sitei256 – 2561NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 126NADPBy similarity

    GO - Molecular functioni

    1. 2-dehydropantoate 2-reductase activity Source: UniProtKB-EC
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. pantothenate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pantothenate biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-435-MONOMER.
    UniPathwayiUPA00028; UER00004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-dehydropantoate 2-reductase (EC:1.1.1.169)
    Alternative name(s):
    Ketopantoate reductase
    Short name:
    KPA reductase
    Short name:
    KPR
    Gene namesi
    Name:panE
    Synonyms:apbA
    Ordered Locus Names:STM0434
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3033032-dehydropantoate 2-reductasePRO_0000157304Add
    BLAST

    Proteomic databases

    PaxDbiP37402.
    PRIDEiP37402.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi99287.STM0434.

    Structurei

    3D structure databases

    ProteinModelPortaliP37402.
    SMRiP37402. Positions 1-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ketopantoate reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG1893.
    HOGENOMiHOG000050223.
    KOiK00077.
    OMAiIEFINGW.
    OrthoDBiEOG68SVW3.
    PhylomeDBiP37402.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR003710. ApbA.
    IPR013328. DH_multihelical.
    IPR013752. KPA_reductase.
    IPR013332. KPR_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02558. ApbA. 1 hit.
    PF08546. ApbA_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00745. apbA_panE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37402-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKITVLGCGA LGQLWLSALC KHGHDVQGWL RVPQPYCSVN LIDTDGSFFN    50
    ESLTANDPDF LAKSELLLVT LKAWQVSDAV RTLASTLPVT SPILLIHNGM 100
    GTIEELQNIQ QPMLMGTITH AARRDGNIII HVANGTTHIG PAREQDGDYS 150
    YLADILQGVL PDVAWHNNIR AEMWRKLAVN CVINPLTALW NCPNGELRHH 200
    TDEINAICEE VAAVIEREGY HTSADDLRYY VEQVIDSTAE NISSMLQDVR 250
    AMRHTEIDYI TGYLLKRARV HGLAVPENSR LFEMVKRKES EYERSGTGMP 300
    RPW 303
    Length:303
    Mass (Da):33,938
    Last modified:January 23, 2002 - v2
    Checksum:i060DA21B75B891A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 8613WQVSD…TLAST → GFRRSTNPGVN in AAA56681. (PubMed:7519593)CuratedAdd
    BLAST
    Sequence conflicti124 – 1241Missing in AAA56681. (PubMed:7519593)Curated
    Sequence conflicti246 – 2472LQ → FE in AAA56681. (PubMed:7519593)Curated
    Sequence conflicti275 – 30329VPENS…MPRPW → FRKIAACLKW in AAA56681. (PubMed:7519593)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211A → T in strain: DM4593.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09529 Genomic DNA. Translation: AAA56681.1.
    AE006468 Genomic DNA. Translation: AAL19388.1.
    PIRiA55849.
    RefSeqiNP_459429.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL19388; AAL19388; STM0434.
    GeneIDi1251953.
    KEGGistm:STM0434.
    PATRICi32379203. VBISalEnt20916_0463.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09529 Genomic DNA. Translation: AAA56681.1 .
    AE006468 Genomic DNA. Translation: AAL19388.1 .
    PIRi A55849.
    RefSeqi NP_459429.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P37402.
    SMRi P37402. Positions 1-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM0434.

    Proteomic databases

    PaxDbi P37402.
    PRIDEi P37402.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL19388 ; AAL19388 ; STM0434 .
    GeneIDi 1251953.
    KEGGi stm:STM0434.
    PATRICi 32379203. VBISalEnt20916_0463.

    Phylogenomic databases

    eggNOGi COG1893.
    HOGENOMi HOG000050223.
    KOi K00077.
    OMAi IEFINGW.
    OrthoDBi EOG68SVW3.
    PhylomeDBi P37402.

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00004 .
    BioCyci SENT99287:GCTI-435-MONOMER.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR003710. ApbA.
    IPR013328. DH_multihelical.
    IPR013752. KPA_reductase.
    IPR013332. KPR_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF02558. ApbA. 1 hit.
    PF08546. ApbA_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00745. apbA_panE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "apbA, a new genetic locus involved in thiamine biosynthesis in Salmonella typhimurium."
      Downs D.M., Petersen L.
      J. Bacteriol. 176:4858-4864(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LT2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway."
      Frodyma M.E., Downs D.M.
      J. Biol. Chem. 273:5572-5576(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    4. "The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium."
      Frodyma M.E., Downs D.M.
      J. Bacteriol. 180:4757-4759(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SHOWS THAT APBA IS PANE.

    Entry informationi

    Entry nameiPANE_SALTY
    AccessioniPrimary (citable) accession number: P37402
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3