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P0A7F3

- PYRI_ECOLI

UniProt

P0A7F3 - PYRI_ECOLI

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Protein
Aspartate carbamoyltransferase regulatory chain
Gene
pyrI, b4244, JW4203
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in allosteric regulation of aspartate carbamoyltransferase.UniRule annotation

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 153152Aspartate carbamoyltransferase regulatory chainUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP0A7F3.

Family & Domainsi

Sequence similaritiesi

Belongs to the PyrI family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 95 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

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