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Protein

Aspartate carbamoyltransferase catalytic chain

Gene

pyrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase catalytic chain (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

GO - Molecular functioni

GO - Biological processi

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.
BRENDAi2.1.3.2. 2026.
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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10805. pyrB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved4 Publications
Chaini2 – 311310Aspartate carbamoyltransferase catalytic chainPRO_0000113128Add
BLAST

Proteomic databases

PaxDbiP0A786.
PRIDEiP0A786.

2D gel databases

SWISS-2DPAGEP0A786.

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

BioGridi4260722. 10 interactions.
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 – 2403Combined sources
Helixi241 – 2444Combined 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-ray3.00A2-311[»]
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[»]
4WTOX-ray2.03A/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

eggNOGiENOG4105CXT. Bacteria.
COG0540. LUCA.
HOGENOMiHOG000022685.
InParanoidiP0A786.
KOiK00609.
OMAiMHPGPMV.
PhylomeDBiP0A786.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr. 1 hit.
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.
WP_000013046.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77202; AAC77202; b4245.
BAE78244; BAE78244; BAE78244.
GeneIDi948767.
KEGGiecj:JW4204.
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.
PIRiH65236. DTECC.
RefSeqiNP_418666.1. NC_000913.3.
WP_000013046.1. NZ_LN832404.1.

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-ray3.00A2-311[»]
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[»]
4WTOX-ray2.03A/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...

Protein-protein interaction databases

BioGridi4260722. 10 interactions.
DIPiDIP-35089N.
IntActiP0A786. 3 interactions.
MINTiMINT-1541312.
STRINGi511145.b4245.

2D gel databases

SWISS-2DPAGEP0A786.

Proteomic databases

PaxDbiP0A786.
PRIDEiP0A786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77202; AAC77202; b4245.
BAE78244; BAE78244; BAE78244.
GeneIDi948767.
KEGGiecj:JW4204.
eco:b4245.
PATRICi32124067. VBIEscCol129921_4378.

Organism-specific databases

EchoBASEiEB0798.
EcoGeneiEG10805. pyrB.

Phylogenomic databases

eggNOGiENOG4105CXT. Bacteria.
COG0540. LUCA.
HOGENOMiHOG000022685.
InParanoidiP0A786.
KOiK00609.
OMAiMHPGPMV.
PhylomeDBiP0A786.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00116.
BioCyciEcoCyc:ASPCARBCAT-MONOMER.
ECOL316407:JW4204-MONOMER.
MetaCyc:ASPCARBCAT-MONOMER.
BRENDAi2.1.3.2. 2026.
SABIO-RKP0A786.

Miscellaneous databases

EvolutionaryTraceiP0A786.
PROiP0A786.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr. 1 hit.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.