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P0A7F3

- PYRI_ECOLI

UniProt

P0A7F3 - PYRI_ECOLI

Protein

Aspartate carbamoyltransferase regulatory chain

Gene

pyrI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in allosteric regulation of aspartate carbamoyltransferase.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi109 – 1091Zinc
    Metal bindingi114 – 1141Zinc
    Metal bindingi138 – 1381Zinc
    Metal bindingi141 – 1411Zinc

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
    2. pyrimidine nucleotide biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:ASPCARBREG-MONOMER.
    ECOL316407:JW4203-MONOMER.
    MetaCyc:ASPCARBREG-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate carbamoyltransferase regulatory chain
    Gene namesi
    Name:pyrI
    Ordered Locus Names:b4244, JW4203
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10811. pyrI.

    Subcellular locationi

    GO - Cellular componenti

    1. aspartate carbamoyltransferase complex Source: InterPro
    2. cytoplasm Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 153152Aspartate carbamoyltransferase regulatory chainPRO_0000142303Add
    BLAST

    Proteomic databases

    PaxDbiP0A7F3.
    PRIDEiP0A7F3.

    2D gel databases

    SWISS-2DPAGEP0A7F3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7F3.

    Interactioni

    Subunit structurei

    Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    pyrBP0A78614EBI-906630,EBI-906620

    Protein-protein interaction databases

    DIPiDIP-35088N.
    IntActiP0A7F3. 2 interactions.
    MINTiMINT-1541364.
    STRINGi511145.b4244.

    Structurei

    Secondary structure

    1
    153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Beta strandi13 – 219
    Turni23 – 253
    Helixi26 – 327
    Turni33 – 364
    Beta strandi37 – 404
    Beta strandi42 – 509
    Turni51 – 533
    Beta strandi54 – 629
    Helixi68 – 725
    Turni73 – 775
    Beta strandi78 – 803
    Beta strandi82 – 876
    Beta strandi90 – 956
    Beta strandi101 – 1066
    Beta strandi112 – 1143
    Turni115 – 1184
    Beta strandi119 – 1213
    Beta strandi124 – 1296
    Beta strandi131 – 1388
    Turni139 – 1413
    Beta strandi144 – 1463
    Helixi147 – 1526

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ACMX-ray2.80B/D1-153[»]
    1AT1X-ray2.80B/D1-153[»]
    1D09X-ray2.10B/D1-153[»]
    1EZZX-ray2.70B/D1-153[»]
    1F1BX-ray2.30B/D1-153[»]
    1I5OX-ray2.80B/D1-153[»]
    1NBEX-ray2.60B/D1-153[»]
    1Q95X-ray2.46G/H/I/J/K/L1-153[»]
    1R0BX-ray2.90G/H/I/J/K/L1-153[»]
    1R0CX-ray2.37B/H1-153[»]
    1RAAX-ray2.50B/D1-153[»]
    1RABX-ray2.50B/D1-153[»]
    1RACX-ray2.50B/D1-153[»]
    1RADX-ray2.50B/D1-153[»]
    1RAEX-ray2.50B/D1-153[»]
    1RAFX-ray2.50B/D1-153[»]
    1RAGX-ray2.50B/D1-153[»]
    1RAHX-ray2.50B/D1-153[»]
    1RAIX-ray2.50B/D1-153[»]
    1SKUX-ray2.60B/D1-153[»]
    1TTHX-ray2.80B/D1-153[»]
    1TU0X-ray2.55B/D1-153[»]
    1TUGX-ray2.10B/D1-153[»]
    1XJWX-ray2.71B/D1-153[»]
    1ZA1X-ray2.20B/D1-153[»]
    1ZA2X-ray2.50B/D1-153[»]
    2A0FX-ray2.90B/D1-153[»]
    2AIRX-ray2.00B/H1-153[»]
    2AT1X-ray2.80B/D1-153[»]
    2ATCX-ray3.00B6-152[»]
    2FZCX-ray2.10B/D1-153[»]
    2FZGX-ray2.25B/D1-153[»]
    2FZKX-ray2.50B/D1-153[»]
    2H3EX-ray2.30B/D1-153[»]
    2HSEX-ray2.60B/D1-153[»]
    2IPOX-ray2.60B/D1-153[»]
    2QG9X-ray2.70B/D1-153[»]
    2QGFX-ray2.20B/D1-153[»]
    3AT1X-ray2.80B/D1-153[»]
    3D7SX-ray2.80B/D1-153[»]
    3MPUX-ray2.86B/D/F1-153[»]
    4AT1X-ray2.60B/D1-153[»]
    4E2FX-ray2.80B/D/F/H/J/L1-153[»]
    4F04X-ray2.30B/D1-153[»]
    4FYVX-ray2.10B/D1-153[»]
    4FYWX-ray2.10B/D1-153[»]
    4FYXX-ray2.09B/D1-153[»]
    4FYYX-ray1.94B/D1-153[»]
    5AT1X-ray2.60B/D1-153[»]
    6AT1X-ray2.60B/D1-153[»]
    7AT1X-ray2.80B/D1-153[»]
    8AT1X-ray2.80B/D1-153[»]
    8ATCX-ray2.50B/D1-153[»]
    9ATCX-ray2.40B8-153[»]
    ProteinModelPortaliP0A7F3.
    SMRiP0A7F3. Positions 6-153.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7F3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PyrI family.Curated

    Phylogenomic databases

    eggNOGiCOG1781.
    HOGENOMiHOG000113530.
    KOiK00610.
    OMAiCITSIEQ.
    OrthoDBiEOG6JX7QS.
    PhylomeDBiP0A7F3.

    Family and domain databases

    Gene3Di2.30.30.20. 1 hit.
    3.30.70.140. 1 hit.
    HAMAPiMF_00002. Asp_carb_tr_reg.
    InterProiIPR020545. Asp_carbamoyltransf_reg_N.
    IPR002801. Asp_carbamoylTrfase_reg.
    IPR020542. Asp_carbamoyltrfase_reg_C.
    [Graphical view]
    PfamiPF01948. PyrI. 1 hit.
    PF02748. PyrI_C. 1 hit.
    [Graphical view]
    ProDomiPD006194. Asp_carbamoylTrfase_reg. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF54893. SSF54893. 1 hit.
    SSF57825. SSF57825. 1 hit.
    TIGRFAMsiTIGR00240. ATCase_reg. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A7F3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHDNKLQVE AIKRGTVIDH IPAQIGFKLL SLFKLTETDQ RITIGLNLPS    50
    GEMGRKDLIK IENTFLSEDQ VDQLALYAPQ ATVNRIDNYE VVGKSRPSLP 100
    ERIDNVLVCP NSNCISHAEP VSSSFAVRKR ANDIALKCKY CEKEFSHNVV 150
    LAN 153
    Length:153
    Mass (Da):17,121
    Last modified:January 23, 2007 - v2
    Checksum:i81A1631614E549EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01472 Genomic DNA. Translation: AAA24477.1.
    U14003 Genomic DNA. Translation: AAA97141.1.
    U00096 Genomic DNA. Translation: AAC77201.1.
    AP009048 Genomic DNA. Translation: BAE78243.1.
    M28578 Genomic DNA. Translation: AAA24487.1.
    PIRiA93985. DTECR.
    RefSeqiNP_418665.1. NC_000913.3.
    YP_492384.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77201; AAC77201; b4244.
    BAE78243; BAE78243; BAE78243.
    GeneIDi12934123.
    948763.
    KEGGiecj:Y75_p4129.
    eco:b4244.
    PATRICi32124065. VBIEscCol129921_4377.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01472 Genomic DNA. Translation: AAA24477.1 .
    U14003 Genomic DNA. Translation: AAA97141.1 .
    U00096 Genomic DNA. Translation: AAC77201.1 .
    AP009048 Genomic DNA. Translation: BAE78243.1 .
    M28578 Genomic DNA. Translation: AAA24487.1 .
    PIRi A93985. DTECR.
    RefSeqi NP_418665.1. NC_000913.3.
    YP_492384.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ACM X-ray 2.80 B/D 1-153 [» ]
    1AT1 X-ray 2.80 B/D 1-153 [» ]
    1D09 X-ray 2.10 B/D 1-153 [» ]
    1EZZ X-ray 2.70 B/D 1-153 [» ]
    1F1B X-ray 2.30 B/D 1-153 [» ]
    1I5O X-ray 2.80 B/D 1-153 [» ]
    1NBE X-ray 2.60 B/D 1-153 [» ]
    1Q95 X-ray 2.46 G/H/I/J/K/L 1-153 [» ]
    1R0B X-ray 2.90 G/H/I/J/K/L 1-153 [» ]
    1R0C X-ray 2.37 B/H 1-153 [» ]
    1RAA X-ray 2.50 B/D 1-153 [» ]
    1RAB X-ray 2.50 B/D 1-153 [» ]
    1RAC X-ray 2.50 B/D 1-153 [» ]
    1RAD X-ray 2.50 B/D 1-153 [» ]
    1RAE X-ray 2.50 B/D 1-153 [» ]
    1RAF X-ray 2.50 B/D 1-153 [» ]
    1RAG X-ray 2.50 B/D 1-153 [» ]
    1RAH X-ray 2.50 B/D 1-153 [» ]
    1RAI X-ray 2.50 B/D 1-153 [» ]
    1SKU X-ray 2.60 B/D 1-153 [» ]
    1TTH X-ray 2.80 B/D 1-153 [» ]
    1TU0 X-ray 2.55 B/D 1-153 [» ]
    1TUG X-ray 2.10 B/D 1-153 [» ]
    1XJW X-ray 2.71 B/D 1-153 [» ]
    1ZA1 X-ray 2.20 B/D 1-153 [» ]
    1ZA2 X-ray 2.50 B/D 1-153 [» ]
    2A0F X-ray 2.90 B/D 1-153 [» ]
    2AIR X-ray 2.00 B/H 1-153 [» ]
    2AT1 X-ray 2.80 B/D 1-153 [» ]
    2ATC X-ray 3.00 B 6-152 [» ]
    2FZC X-ray 2.10 B/D 1-153 [» ]
    2FZG X-ray 2.25 B/D 1-153 [» ]
    2FZK X-ray 2.50 B/D 1-153 [» ]
    2H3E X-ray 2.30 B/D 1-153 [» ]
    2HSE X-ray 2.60 B/D 1-153 [» ]
    2IPO X-ray 2.60 B/D 1-153 [» ]
    2QG9 X-ray 2.70 B/D 1-153 [» ]
    2QGF X-ray 2.20 B/D 1-153 [» ]
    3AT1 X-ray 2.80 B/D 1-153 [» ]
    3D7S X-ray 2.80 B/D 1-153 [» ]
    3MPU X-ray 2.86 B/D/F 1-153 [» ]
    4AT1 X-ray 2.60 B/D 1-153 [» ]
    4E2F X-ray 2.80 B/D/F/H/J/L 1-153 [» ]
    4F04 X-ray 2.30 B/D 1-153 [» ]
    4FYV X-ray 2.10 B/D 1-153 [» ]
    4FYW X-ray 2.10 B/D 1-153 [» ]
    4FYX X-ray 2.09 B/D 1-153 [» ]
    4FYY X-ray 1.94 B/D 1-153 [» ]
    5AT1 X-ray 2.60 B/D 1-153 [» ]
    6AT1 X-ray 2.60 B/D 1-153 [» ]
    7AT1 X-ray 2.80 B/D 1-153 [» ]
    8AT1 X-ray 2.80 B/D 1-153 [» ]
    8ATC X-ray 2.50 B/D 1-153 [» ]
    9ATC X-ray 2.40 B 8-153 [» ]
    ProteinModelPortali P0A7F3.
    SMRi P0A7F3. Positions 6-153.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35088N.
    IntActi P0A7F3. 2 interactions.
    MINTi MINT-1541364.
    STRINGi 511145.b4244.

    2D gel databases

    SWISS-2DPAGE P0A7F3.

    Proteomic databases

    PaxDbi P0A7F3.
    PRIDEi P0A7F3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77201 ; AAC77201 ; b4244 .
    BAE78243 ; BAE78243 ; BAE78243 .
    GeneIDi 12934123.
    948763.
    KEGGi ecj:Y75_p4129.
    eco:b4244.
    PATRICi 32124065. VBIEscCol129921_4377.

    Organism-specific databases

    EchoBASEi EB0804.
    EcoGenei EG10811. pyrI.

    Phylogenomic databases

    eggNOGi COG1781.
    HOGENOMi HOG000113530.
    KOi K00610.
    OMAi CITSIEQ.
    OrthoDBi EOG6JX7QS.
    PhylomeDBi P0A7F3.

    Enzyme and pathway databases

    BioCyci EcoCyc:ASPCARBREG-MONOMER.
    ECOL316407:JW4203-MONOMER.
    MetaCyc:ASPCARBREG-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7F3.
    PROi P0A7F3.

    Gene expression databases

    Genevestigatori P0A7F3.

    Family and domain databases

    Gene3Di 2.30.30.20. 1 hit.
    3.30.70.140. 1 hit.
    HAMAPi MF_00002. Asp_carb_tr_reg.
    InterProi IPR020545. Asp_carbamoyltransf_reg_N.
    IPR002801. Asp_carbamoylTrfase_reg.
    IPR020542. Asp_carbamoyltrfase_reg_C.
    [Graphical view ]
    Pfami PF01948. PyrI. 1 hit.
    PF02748. PyrI_C. 1 hit.
    [Graphical view ]
    ProDomi PD006194. Asp_carbamoylTrfase_reg. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF54893. SSF54893. 1 hit.
    SSF57825. SSF57825. 1 hit.
    TIGRFAMsi TIGR00240. ATCase_reg. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Location of amino acid alterations in mutants of aspartate transcarbamoylase: structural aspects of interallelic complementation."
      Schachman H.K., Pauza C.D., Navre M., Karels M.J., Wu L., Yang Y.R.
      Proc. Natl. Acad. Sci. U.S.A. 81:115-119(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: PROTEIN SEQUENCE OF 2-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    7. "Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. I. Primary structure of a pyrI gene encoding a modified regulatory subunit."
      Cunin R., Jacobs A., Charlier D.R.M., Crabeel M., Herve G., Glansdorff N., Pierard A.
      J. Mol. Biol. 186:707-713(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-153.
    8. "New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain."
      Weber K.
      Nature 218:1116-1119(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-153.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate."
      Monaco H.L., Crawford J.L., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 75:5276-5280(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    11. "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution."
      Ke H.-M., Honzatko R.B., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 81:4037-4040(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
    12. "Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution."
      Stevens R.C., Gouaux J.E., Lipscomb W.N.
      Biochemistry 29:7691-7701(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    13. "Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH."
      Gouaux J.E., Stevens R.C., Lipscomb W.N.
      Biochemistry 29:7702-7715(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiPYRI_ECOLI
    AccessioniPrimary (citable) accession number: P0A7F3
    Secondary accession number(s): P00478, Q2M663
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 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

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3