Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A786

- PYRB_ECOLI

UniProt

P0A786 - PYRB_ECOLI

Protein

Aspartate carbamoyltransferase catalytic chain

Gene

pyrB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. aspartate carbamoyltransferase activity Source: UniProtKB-HAMAP
    3. protein binding Source: IntAct

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
    2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    3. cellular amino acid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:ASPCARBCAT-MONOMER.
    ECOL316407:JW4204-MONOMER.
    MetaCyc:ASPCARBCAT-MONOMER.
    SABIO-RKP0A786.
    UniPathwayiUPA00070; UER00116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate carbamoyltransferase catalytic chain (EC:2.1.3.2)
    Alternative name(s):
    Aspartate transcarbamylase
    Short name:
    ATCase
    Gene namesi
    Name:pyrB
    Ordered Locus Names:b4245, JW4204
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10805. pyrB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 311310Aspartate carbamoyltransferase catalytic chainPRO_0000113128Add
    BLAST

    Proteomic databases

    PaxDbiP0A786.
    PRIDEiP0A786.

    2D gel databases

    SWISS-2DPAGEP0A786.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A786.

    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
    pyrIP0A7F314EBI-906620,EBI-906630

    Protein-protein interaction databases

    DIPiDIP-35089N.
    IntActiP0A786. 3 interactions.
    MINTiMINT-1541312.
    STRINGi511145.b4245.

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 74
    Helixi13 – 153
    Helixi18 – 3316
    Turni37 – 426
    Beta strandi44 – 518
    Helixi54 – 6512
    Turni66 – 683
    Beta strandi70 – 756
    Helixi77 – 793
    Turni80 – 823
    Helixi86 – 9611
    Turni97 – 993
    Beta strandi101 – 1099
    Helixi112 – 1198
    Beta strandi120 – 1223
    Beta strandi125 – 1306
    Turni131 – 1333
    Helixi136 – 15015
    Beta strandi153 – 1553
    Beta strandi157 – 1626
    Turni164 – 1663
    Helixi168 – 17811
    Beta strandi180 – 1823
    Beta strandi184 – 1885
    Helixi191 – 1933
    Helixi197 – 2059
    Beta strandi210 – 2123
    Helixi216 – 2183
    Turni219 – 2224
    Beta strandi224 – 2285
    Helixi233 – 2353
    Helixi238 – 2447
    Helixi245 – 2473
    Beta strandi248 – 2503
    Helixi252 – 2554
    Beta strandi256 – 2583
    Beta strandi263 – 2653
    Beta strandi271 – 2744
    Helixi276 – 2794
    Beta strandi281 – 2844
    Helixi286 – 2916
    Helixi293 – 30513
    Beta strandi306 – 3083

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ACMX-ray2.80A/C2-311[»]
    1AT1X-ray2.80A/C2-311[»]
    1D09X-ray2.10A/C2-311[»]
    1EKXX-ray1.95A/B/C1-311[»]
    1EZZX-ray2.70A/C2-311[»]
    1F1BX-ray2.30A/C2-311[»]
    1GQ3X-ray2.01A/B/C2-311[»]
    1I5OX-ray2.80A/C2-311[»]
    1NBEX-ray2.60A/C2-311[»]
    1Q95X-ray2.46A/B/C/D/E/F2-311[»]
    1R0BX-ray2.90A/B/C/D/E/F2-311[»]
    1R0CX-ray2.37A/G2-311[»]
    1RAAX-ray2.50A/C2-311[»]
    1RABX-ray2.50A/C2-311[»]
    1RACX-ray2.50A/C2-311[»]
    1RADX-ray2.50A/C2-311[»]
    1RAEX-ray2.50A/C2-311[»]
    1RAFX-ray2.50A/C2-311[»]
    1RAGX-ray2.50A/C2-311[»]
    1RAHX-ray2.50A/C2-311[»]
    1RAIX-ray2.50A/C2-311[»]
    1SKUX-ray2.60A/C2-311[»]
    1TTHX-ray2.80A/C2-311[»]
    1TU0X-ray2.55A/C2-311[»]
    1TUGX-ray2.10A/C2-311[»]
    1XJWX-ray2.71A/C2-311[»]
    1ZA1X-ray2.20A/C2-311[»]
    1ZA2X-ray2.50A/C2-311[»]
    2A0FX-ray2.90A/C2-311[»]
    2AIRX-ray2.00A/G2-311[»]
    2AT1X-ray2.80A/C2-311[»]
    2ATCX-ray3.00A2-310[»]
    2FZCX-ray2.10A/C2-311[»]
    2FZGX-ray2.25A/C2-311[»]
    2FZKX-ray2.50A/C2-311[»]
    2H3EX-ray2.30A/C2-311[»]
    2HSEX-ray2.60A/C2-311[»]
    2IPOX-ray2.60A/C2-311[»]
    2QG9X-ray2.70A/C2-311[»]
    2QGFX-ray2.20A/C2-311[»]
    3AT1X-ray2.80A/C2-311[»]
    3CSUX-ray1.88A/B/C2-311[»]
    3D7SX-ray2.80A/C2-311[»]
    3MPUX-ray2.86A/C/E2-311[»]
    3NPMX-ray2.10A2-311[»]
    4AT1X-ray2.60A/C2-311[»]
    4E2FX-ray2.80A/C/E/G/I/K2-311[»]
    4F04X-ray2.30A/C2-311[»]
    4FYVX-ray2.10A/C2-311[»]
    4FYWX-ray2.10A/C2-311[»]
    4FYXX-ray2.09A/C2-311[»]
    4FYYX-ray1.94A/C2-311[»]
    5AT1X-ray2.60A/C2-311[»]
    6AT1X-ray2.60A/C2-311[»]
    7AT1X-ray2.80A/C2-311[»]
    8AT1X-ray2.80A/C2-311[»]
    8ATCX-ray2.50A/C2-311[»]
    9ATCX-ray2.40A2-311[»]
    ProteinModelPortaliP0A786.
    SMRiP0A786. Positions 2-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A786.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family.Curated

    Phylogenomic databases

    eggNOGiCOG0540.
    HOGENOMiHOG000022685.
    KOiK00609.
    OMAiVIYVTRI.
    OrthoDBiEOG61KBJZ.
    PhylomeDBiP0A786.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_00001. Asp_carb_tr.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR002082. Asp_carbamoyltransf.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    [Graphical view]
    PfamiPF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view]
    PRINTSiPR00100. AOTCASE.
    PR00101. ATCASE.
    SUPFAMiSSF53671. SSF53671. 1 hit.
    TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
    PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A786-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANPLYQKHI ISINDLSRDD LNLVLATAAK LKANPQPELL KHKVIASCFF    50
    EASTRTRLSF ETSMHRLGAS VVGFSDSANT SLGKKGETLA DTISVISTYV 100
    DAIVMRHPQE GAARLATEFS GNVPVLNAGD GSNQHPTQTL LDLFTIQETQ 150
    GRLDNLHVAM VGDLKYGRTV HSLTQALAKF DGNRFYFIAP DALAMPQYIL 200
    DMLDEKGIAW SLHSSIEEVM AEVDILYMTR VQKERLDPSE YANVKAQFVL 250
    RASDLHNAKA NMKVLHPLPR VDEIATDVDK TPHAWYFQQA GNGIFARQAL 300
    LALVLNRDLV L 311
    Length:311
    Mass (Da):34,427
    Last modified:January 23, 2007 - v2
    Checksum:iCC2F5ACBD73E0E3E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611E → Q(PubMed:6302686)Curated
    Sequence conflicti61 – 611E → Q AA sequence (PubMed:6341995)Curated
    Sequence conflicti87 – 871E → Q AA sequence (PubMed:6341995)Curated
    Sequence conflicti91 – 911D → N AA sequence (PubMed:6341995)Curated
    Sequence conflicti130 – 1301D → N AA sequence (PubMed:6341995)Curated
    Sequence conflicti150 – 1501Q → E in AAA24476. (PubMed:6364131)Curated
    Sequence conflicti196 – 1961P → R in AAA97142. (PubMed:7610040)Curated
    Sequence conflicti221 – 2211A → V(PubMed:6302686)Curated
    Sequence conflicti221 – 2211A → V AA sequence (PubMed:6341995)Curated
    Sequence conflicti257 – 2571N → D AA sequence (PubMed:6341995)Curated
    Sequence conflicti260 – 2623ANM → MNA AA sequence (PubMed:6341995)Curated
    Sequence conflicti297 – 2971R → L in AAA24474. (PubMed:6302686)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01670 Genomic DNA. Translation: AAA24474.1.
    K01472 Genomic DNA. Translation: AAA24476.1.
    U14003 Genomic DNA. Translation: AAA97142.1.
    U00096 Genomic DNA. Translation: AAC77202.1.
    AP009048 Genomic DNA. Translation: BAE78244.1.
    M10743 Genomic DNA. Translation: AAA24479.1.
    M60508 Genomic DNA. Translation: AAA24481.1.
    PIRiH65236. DTECC.
    RefSeqiNP_418666.1. NC_000913.3.
    YP_492385.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77202; AAC77202; b4245.
    BAE78244; BAE78244; BAE78244.
    GeneIDi12931728.
    948767.
    KEGGiecj:Y75_p4130.
    eco:b4245.
    PATRICi32124067. VBIEscCol129921_4378.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01670 Genomic DNA. Translation: AAA24474.1 .
    K01472 Genomic DNA. Translation: AAA24476.1 .
    U14003 Genomic DNA. Translation: AAA97142.1 .
    U00096 Genomic DNA. Translation: AAC77202.1 .
    AP009048 Genomic DNA. Translation: BAE78244.1 .
    M10743 Genomic DNA. Translation: AAA24479.1 .
    M60508 Genomic DNA. Translation: AAA24481.1 .
    PIRi H65236. DTECC.
    RefSeqi NP_418666.1. NC_000913.3.
    YP_492385.1. 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 A/C 2-311 [» ]
    1AT1 X-ray 2.80 A/C 2-311 [» ]
    1D09 X-ray 2.10 A/C 2-311 [» ]
    1EKX X-ray 1.95 A/B/C 1-311 [» ]
    1EZZ X-ray 2.70 A/C 2-311 [» ]
    1F1B X-ray 2.30 A/C 2-311 [» ]
    1GQ3 X-ray 2.01 A/B/C 2-311 [» ]
    1I5O X-ray 2.80 A/C 2-311 [» ]
    1NBE X-ray 2.60 A/C 2-311 [» ]
    1Q95 X-ray 2.46 A/B/C/D/E/F 2-311 [» ]
    1R0B X-ray 2.90 A/B/C/D/E/F 2-311 [» ]
    1R0C X-ray 2.37 A/G 2-311 [» ]
    1RAA X-ray 2.50 A/C 2-311 [» ]
    1RAB X-ray 2.50 A/C 2-311 [» ]
    1RAC X-ray 2.50 A/C 2-311 [» ]
    1RAD X-ray 2.50 A/C 2-311 [» ]
    1RAE X-ray 2.50 A/C 2-311 [» ]
    1RAF X-ray 2.50 A/C 2-311 [» ]
    1RAG X-ray 2.50 A/C 2-311 [» ]
    1RAH X-ray 2.50 A/C 2-311 [» ]
    1RAI X-ray 2.50 A/C 2-311 [» ]
    1SKU X-ray 2.60 A/C 2-311 [» ]
    1TTH X-ray 2.80 A/C 2-311 [» ]
    1TU0 X-ray 2.55 A/C 2-311 [» ]
    1TUG X-ray 2.10 A/C 2-311 [» ]
    1XJW X-ray 2.71 A/C 2-311 [» ]
    1ZA1 X-ray 2.20 A/C 2-311 [» ]
    1ZA2 X-ray 2.50 A/C 2-311 [» ]
    2A0F X-ray 2.90 A/C 2-311 [» ]
    2AIR X-ray 2.00 A/G 2-311 [» ]
    2AT1 X-ray 2.80 A/C 2-311 [» ]
    2ATC X-ray 3.00 A 2-310 [» ]
    2FZC X-ray 2.10 A/C 2-311 [» ]
    2FZG X-ray 2.25 A/C 2-311 [» ]
    2FZK X-ray 2.50 A/C 2-311 [» ]
    2H3E X-ray 2.30 A/C 2-311 [» ]
    2HSE X-ray 2.60 A/C 2-311 [» ]
    2IPO X-ray 2.60 A/C 2-311 [» ]
    2QG9 X-ray 2.70 A/C 2-311 [» ]
    2QGF X-ray 2.20 A/C 2-311 [» ]
    3AT1 X-ray 2.80 A/C 2-311 [» ]
    3CSU X-ray 1.88 A/B/C 2-311 [» ]
    3D7S X-ray 2.80 A/C 2-311 [» ]
    3MPU X-ray 2.86 A/C/E 2-311 [» ]
    3NPM X-ray 2.10 A 2-311 [» ]
    4AT1 X-ray 2.60 A/C 2-311 [» ]
    4E2F X-ray 2.80 A/C/E/G/I/K 2-311 [» ]
    4F04 X-ray 2.30 A/C 2-311 [» ]
    4FYV X-ray 2.10 A/C 2-311 [» ]
    4FYW X-ray 2.10 A/C 2-311 [» ]
    4FYX X-ray 2.09 A/C 2-311 [» ]
    4FYY X-ray 1.94 A/C 2-311 [» ]
    5AT1 X-ray 2.60 A/C 2-311 [» ]
    6AT1 X-ray 2.60 A/C 2-311 [» ]
    7AT1 X-ray 2.80 A/C 2-311 [» ]
    8AT1 X-ray 2.80 A/C 2-311 [» ]
    8ATC X-ray 2.50 A/C 2-311 [» ]
    9ATC X-ray 2.40 A 2-311 [» ]
    ProteinModelPortali P0A786.
    SMRi P0A786. Positions 2-311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35089N.
    IntActi P0A786. 3 interactions.
    MINTi MINT-1541312.
    STRINGi 511145.b4245.

    2D gel databases

    SWISS-2DPAGE P0A786.

    Proteomic databases

    PaxDbi P0A786.
    PRIDEi P0A786.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77202 ; AAC77202 ; b4245 .
    BAE78244 ; BAE78244 ; BAE78244 .
    GeneIDi 12931728.
    948767.
    KEGGi ecj:Y75_p4130.
    eco:b4245.
    PATRICi 32124067. VBIEscCol129921_4378.

    Organism-specific databases

    EchoBASEi EB0798.
    EcoGenei EG10805. pyrB.

    Phylogenomic databases

    eggNOGi COG0540.
    HOGENOMi HOG000022685.
    KOi K00609.
    OMAi VIYVTRI.
    OrthoDBi EOG61KBJZ.
    PhylomeDBi P0A786.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00116 .
    BioCyci EcoCyc:ASPCARBCAT-MONOMER.
    ECOL316407:JW4204-MONOMER.
    MetaCyc:ASPCARBCAT-MONOMER.
    SABIO-RK P0A786.

    Miscellaneous databases

    EvolutionaryTracei P0A786.
    PROi P0A786.

    Gene expression databases

    Genevestigatori P0A786.

    Family and domain databases

    Gene3Di 3.40.50.1370. 2 hits.
    HAMAPi MF_00001. Asp_carb_tr.
    InterProi IPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR002082. Asp_carbamoyltransf.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    [Graphical view ]
    Pfami PF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00100. AOTCASE.
    PR00101. ATCASE.
    SUPFAMi SSF53671. SSF53671. 1 hit.
    TIGRFAMsi TIGR00670. asp_carb_tr. 1 hit.
    PROSITEi PS00097. CARBAMOYLTRANSFERASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli."
      Hoover T.A., Roof W.D., Foltermann K.F., O'Donovan G.A., Bencini D.A., Wild J.R.
      Proc. Natl. Acad. Sci. U.S.A. 80:2462-2466(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
    3. "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.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 195.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli."
      Konigsberg W.H., Henderson L.
      Proc. Natl. Acad. Sci. U.S.A. 80:2467-2471(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-311.
    7. "Role of the ribosome in suppressing transcriptional termination at the pyrBI attenuator of Escherichia coli K-12."
      Roland K.L., Liu C., Turnbough C.L. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 85:7149-7153(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
    8. "Role of translation and attenuation in the control of pyrBI operon expression in Escherichia coli K-12."
      Roland K.L., Powell F.E., Turnbough C.L. Jr.
      J. Bacteriol. 163:991-999(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
      Strain: K12.
    9. "Attenuation control of pyrBI operon expression in Escherichia coli K-12."
      Turnbough C.L. Jr., Hicks K.L., Donahue J.P.
      Proc. Natl. Acad. Sci. U.S.A. 80:368-372(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
      Strain: K12.
    10. "Characterization of transcriptional initiation from promoters P1 and P2 of the pyrBI operon of Escherichia coli K12."
      Donahue J.P., Turnbough C.L. Jr.
      J. Biol. Chem. 265:19091-19099(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
      Strain: K12.
    11. Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    12. "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 2-21.
      Strain: K12 / EMG2.
    13. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
      Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
      Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    14. "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.
    15. "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.
    16. "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).
    17. "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).
    18. "Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit."
      Beernink P.T., Endrizzi J.A., Alber T., Schachman H.K.
      Proc. Natl. Acad. Sci. U.S.A. 96:5388-5393(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).

    Entry informationi

    Entry nameiPYRB_ECOLI
    AccessioniPrimary (citable) accession number: P0A786
    Secondary accession number(s): P00479
    , Q2M662, Q47555, Q47557
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3