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P0A786

- PYRB_ECOLI

UniProt

P0A786 - PYRB_ECOLI

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A786.
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

        10         20         30         40         50
MANPLYQKHI ISINDLSRDD LNLVLATAAK LKANPQPELL KHKVIASCFF
60 70 80 90 100
EASTRTRLSF ETSMHRLGAS VVGFSDSANT SLGKKGETLA DTISVISTYV
110 120 130 140 150
DAIVMRHPQE GAARLATEFS GNVPVLNAGD GSNQHPTQTL LDLFTIQETQ
160 170 180 190 200
GRLDNLHVAM VGDLKYGRTV HSLTQALAKF DGNRFYFIAP DALAMPQYIL
210 220 230 240 250
DMLDEKGIAW SLHSSIEEVM AEVDILYMTR VQKERLDPSE YANVKAQFVL
260 270 280 290 300
RASDLHNAKA NMKVLHPLPR VDEIATDVDK TPHAWYFQQA GNGIFARQAL
310
LALVLNRDLV L
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P0A786.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 102 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