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P0A7F3 (PYRI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate carbamoyltransferase regulatory chain
Gene names
Name:pyrI
Ordered Locus Names:b4244, JW4203
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in allosteric regulation of aspartate carbamoyltransferase. HAMAP-Rule MF_00002

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2). Ref.11

Sequence similarities

Belongs to the PyrI family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pyrBP0A78614EBI-906630,EBI-906620

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6 Ref.8
Chain2 – 153152Aspartate carbamoyltransferase regulatory chain HAMAP-Rule MF_00002
PRO_0000142303

Sites

Metal binding1091Zinc
Metal binding1141Zinc
Metal binding1381Zinc
Metal binding1411Zinc

Secondary structure

.................................... 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7F3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 81A1631614E549EA

FASTA15317,121
        10         20         30         40         50         60 
MTHDNKLQVE AIKRGTVIDH IPAQIGFKLL SLFKLTETDQ RITIGLNLPS GEMGRKDLIK 

        70         80         90        100        110        120 
IENTFLSEDQ VDQLALYAPQ ATVNRIDNYE VVGKSRPSLP ERIDNVLVCP NSNCISHAEP 

       130        140        150 
VSSSFAVRKR ANDIALKCKY CEKEFSHNVV LAN 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDTECR. A93985.
RefSeqNP_418665.1. NC_000913.3.
YP_492384.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACMX-ray2.80B/D2-152[»]
1AT1X-ray2.80B/D2-152[»]
1D09X-ray2.10B/D1-153[»]
1EZZX-ray2.70B/D1-153[»]
1F1BX-ray2.30B/D1-153[»]
1I5OX-ray2.80B/D1-153[»]
1NBEX-ray2.60B/D2-152[»]
1Q95X-ray2.46G/H/I/J/K/L1-152[»]
1R0BX-ray2.90G/H/I/J/K/L1-152[»]
1R0CX-ray2.37B/H1-152[»]
1RAAX-ray2.50B/D2-152[»]
1RABX-ray2.50B/D2-152[»]
1RACX-ray2.50B/D2-152[»]
1RADX-ray2.50B/D2-152[»]
1RAEX-ray2.50B/D2-152[»]
1RAFX-ray2.50B/D2-152[»]
1RAGX-ray2.50B/D2-152[»]
1RAHX-ray2.50B/D2-152[»]
1RAIX-ray2.50B/D2-152[»]
1SKUX-ray2.60B/D1-152[»]
1TTHX-ray2.80B/D2-152[»]
1TU0X-ray2.55B/D2-152[»]
1TUGX-ray2.10B/D2-152[»]
1XJWX-ray2.71B/D2-152[»]
1ZA1X-ray2.20B/D1-153[»]
1ZA2X-ray2.50B/D1-153[»]
2A0FX-ray2.90B/D2-152[»]
2AIRX-ray2.00B/H1-153[»]
2AT1X-ray2.80B/D2-152[»]
2ATCX-ray3.00B6-152[»]
2FZCX-ray2.10B/D1-152[»]
2FZGX-ray2.25B/D1-152[»]
2FZKX-ray2.50B/D1-152[»]
2H3EX-ray2.30B/D1-152[»]
2HSEX-ray2.60B/D2-152[»]
2IPOX-ray2.60B/D2-152[»]
2QG9X-ray2.70B/D1-153[»]
2QGFX-ray2.20B/D1-153[»]
3AT1X-ray2.80B/D2-152[»]
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/D2-152[»]
9ATCX-ray2.40B8-152[»]
ProteinModelPortalP0A7F3.
SMRP0A7F3. Positions 6-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35088N.
IntActP0A7F3. 2 interactions.
MINTMINT-1541364.
STRING511145.b4244.

2D gel databases

SWISS-2DPAGEP0A7F3.

Proteomic databases

PaxDbP0A7F3.
PRIDEP0A7F3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77201; AAC77201; b4244.
BAE78243; BAE78243; BAE78243.
GeneID12934123.
948763.
KEGGecj:Y75_p4129.
eco:b4244.
PATRIC32124065. VBIEscCol129921_4377.

Organism-specific databases

EchoBASEEB0804.
EcoGeneEG10811. pyrI.

Phylogenomic databases

eggNOGCOG1781.
HOGENOMHOG000113530.
KOK00610.
OMANPNCISN.
OrthoDBEOG6JX7QS.
PhylomeDBP0A7F3.
ProtClustDBPRK00893.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A7F3.

Family and domain databases

Gene3D2.30.30.20. 1 hit.
3.30.70.140. 1 hit.
HAMAPMF_00002. Asp_carb_tr_reg.
InterProIPR020545. Asp_carbamoyltransf_reg_N.
IPR002801. Asp_carbamoylTrfase_reg.
IPR020542. Asp_carbamoyltrfase_reg_C.
[Graphical view]
PfamPF01948. PyrI. 1 hit.
PF02748. PyrI_C. 1 hit.
[Graphical view]
ProDomPD006194. Asp_carbamoylTrfase_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54893. SSF54893. 1 hit.
SSF57825. SSF57825. 1 hit.
TIGRFAMsTIGR00240. ATCase_reg. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A7F3.
PROP0A7F3.

Entry information

Entry namePYRI_ECOLI
AccessionPrimary (citable) accession number: P0A7F3
Secondary accession number(s): P00478, Q2M663
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene