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P0A786 (PYRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 catalytic chain

EC=2.1.3.2
Alternative name(s):
Aspartate transcarbamylase
Short name=ATCase
Gene names
Name:pyrB
Ordered Locus Names:b4245, JW4204
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. HAMAP-Rule MF_00001

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. HAMAP-Rule MF_00001

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.15

Sequence similarities

Belongs to the ATCase/OTCase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pyrIP0A7F314EBI-906620,EBI-906630

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.11 Ref.12 Ref.13
Chain2 – 311310Aspartate carbamoyltransferase catalytic chain HAMAP-Rule MF_00001
PRO_0000113128

Experimental info

Sequence conflict611E → Q Ref.1
Sequence conflict611E → Q AA sequence Ref.6
Sequence conflict871E → Q AA sequence Ref.6
Sequence conflict911D → N AA sequence Ref.6
Sequence conflict1301D → N AA sequence Ref.6
Sequence conflict1501Q → E in AAA24476. Ref.2
Sequence conflict1961P → R in AAA97142. Ref.3
Sequence conflict2211A → V Ref.1
Sequence conflict2211A → V AA sequence Ref.6
Sequence conflict2571N → D AA sequence Ref.6
Sequence conflict260 – 2623ANM → MNA AA sequence Ref.6
Sequence conflict2971R → L in AAA24474. Ref.1

Secondary structure

............................................................................. 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A786 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CC2F5ACBD73E0E3E

FASTA31134,427
        10         20         30         40         50         60 
MANPLYQKHI ISINDLSRDD LNLVLATAAK LKANPQPELL KHKVIASCFF EASTRTRLSF 

        70         80         90        100        110        120 
ETSMHRLGAS VVGFSDSANT SLGKKGETLA DTISVISTYV DAIVMRHPQE GAARLATEFS 

       130        140        150        160        170        180 
GNVPVLNAGD GSNQHPTQTL LDLFTIQETQ GRLDNLHVAM VGDLKYGRTV HSLTQALAKF 

       190        200        210        220        230        240 
DGNRFYFIAP DALAMPQYIL DMLDEKGIAW SLHSSIEEVM AEVDILYMTR VQKERLDPSE 

       250        260        270        280        290        300 
YANVKAQFVL RASDLHNAKA NMKVLHPLPR VDEIATDVDK TPHAWYFQQA GNGIFARQAL 

       310 
LALVLNRDLV L 

« Hide

References

« Hide 'large scale' references
[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]"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], 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]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 2-12.
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDTECC. H65236.
RefSeqNP_418666.1. NC_000913.3.
YP_492385.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACMX-ray2.80A/C2-310[»]
1AT1X-ray2.80A/C2-310[»]
1D09X-ray2.10A/C2-311[»]
1EKXX-ray1.95A/B/C1-311[»]
1EZZX-ray2.70A/C2-310[»]
1F1BX-ray2.30A/C2-310[»]
1GQ3X-ray2.01A/B/C2-311[»]
1I5OX-ray2.80A/C2-310[»]
1NBEX-ray2.60A/C2-310[»]
1Q95X-ray2.46A/B/C/D/E/F2-310[»]
1R0BX-ray2.90A/B/C/D/E/F2-310[»]
1R0CX-ray2.37A/G2-310[»]
1RAAX-ray2.50A/C2-310[»]
1RABX-ray2.50A/C2-310[»]
1RACX-ray2.50A/C2-310[»]
1RADX-ray2.50A/C2-310[»]
1RAEX-ray2.50A/C2-310[»]
1RAFX-ray2.50A/C2-310[»]
1RAGX-ray2.50A/C2-310[»]
1RAHX-ray2.50A/C2-310[»]
1RAIX-ray2.50A/C2-310[»]
1SKUX-ray2.60A/C2-310[»]
1TTHX-ray2.80A/C2-310[»]
1TU0X-ray2.55A/C2-310[»]
1TUGX-ray2.10A/C2-310[»]
1XJWX-ray2.71A/C2-310[»]
1ZA1X-ray2.20A/C2-311[»]
1ZA2X-ray2.50A/C2-311[»]
2A0FX-ray2.90A/C2-310[»]
2AIRX-ray2.00A/G2-310[»]
2AT1X-ray2.80A/C2-310[»]
2ATCX-ray3.00A2-310[»]
2FZCX-ray2.10A/C2-310[»]
2FZGX-ray2.25A/C2-310[»]
2FZKX-ray2.50A/C2-310[»]
2H3EX-ray2.30A/C2-310[»]
2HSEX-ray2.60A/C2-310[»]
2IPOX-ray2.60A/C2-310[»]
2QG9X-ray2.70A/C2-311[»]
2QGFX-ray2.20A/C2-311[»]
3AT1X-ray2.80A/C2-310[»]
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/C2-310[»]
9ATCX-ray2.40A2-310[»]
ProteinModelPortalP0A786.
SMRP0A786. Positions 2-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35089N.
IntActP0A786. 3 interactions.
MINTMINT-1541312.
STRING511145.b4245.

2D gel databases

SWISS-2DPAGEP0A786.

Proteomic databases

PaxDbP0A786.
PRIDEP0A786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77202; AAC77202; b4245.
BAE78244; BAE78244; BAE78244.
GeneID12931728.
948767.
KEGGecj:Y75_p4130.
eco:b4245.
PATRIC32124067. VBIEscCol129921_4378.

Organism-specific databases

EchoBASEEB0798.
EcoGeneEG10805. pyrB.

Phylogenomic databases

eggNOGCOG0540.
HOGENOMHOG000022685.
KOK00609.
OMAKEEYHAR.
OrthoDBEOG61KBJZ.
PhylomeDBP0A786.
ProtClustDBPRK00856.

Enzyme and pathway databases

BioCycEcoCyc:ASPCARBCAT-MONOMER.
ECOL316407:JW4204-MONOMER.
MetaCyc:ASPCARBCAT-MONOMER.
SABIO-RKP0A786.
UniPathwayUPA00070; UER00116.

Gene expression databases

GenevestigatorP0A786.

Family and domain databases

Gene3D3.40.50.1370. 2 hits.
HAMAPMF_00001. Asp_carb_tr.
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMSSF53671. SSF53671. 1 hit.
TIGRFAMsTIGR00670. asp_carb_tr. 1 hit.
PROSITEPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A786.
PROP0A786.

Entry information

Entry namePYRB_ECOLI
AccessionPrimary (citable) accession number: P0A786
Secondary accession number(s): P00479 expand/collapse secondary AC list , Q2M662, Q47555, Q47557
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 96 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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