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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved4 Publications
ChainiPRO_00001131282 – 311Aspartate carbamoyltransferase catalytic chainAdd BLAST310

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 interactors.
DIPiDIP-35089N.
IntActiP0A786. 3 interactors.
MINTiMINT-1541312.
STRINGi511145.b4245.

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Helixi13 – 15Combined sources3
Helixi18 – 33Combined sources16
Turni37 – 42Combined sources6
Beta strandi44 – 51Combined sources8
Helixi54 – 65Combined sources12
Turni66 – 68Combined sources3
Beta strandi70 – 75Combined sources6
Helixi77 – 79Combined sources3
Turni80 – 82Combined sources3
Helixi86 – 96Combined sources11
Turni97 – 99Combined sources3
Beta strandi101 – 109Combined sources9
Helixi112 – 119Combined sources8
Beta strandi120 – 122Combined sources3
Beta strandi125 – 130Combined sources6
Turni131 – 133Combined sources3
Helixi136 – 150Combined sources15
Beta strandi153 – 155Combined sources3
Beta strandi157 – 162Combined sources6
Turni164 – 166Combined sources3
Helixi168 – 178Combined sources11
Beta strandi180 – 182Combined sources3
Beta strandi184 – 188Combined sources5
Helixi191 – 193Combined sources3
Helixi197 – 205Combined sources9
Beta strandi210 – 212Combined sources3
Helixi216 – 218Combined sources3
Turni219 – 222Combined sources4
Beta strandi224 – 228Combined sources5
Helixi233 – 235Combined sources3
Helixi238 – 240Combined sources3
Helixi241 – 244Combined sources4
Helixi245 – 247Combined sources3
Beta strandi248 – 250Combined sources3
Helixi252 – 255Combined sources4
Beta strandi256 – 258Combined sources3
Beta strandi263 – 265Combined sources3
Beta strandi271 – 274Combined sources4
Helixi276 – 279Combined sources4
Beta strandi281 – 284Combined sources4
Helixi286 – 291Combined sources6
Helixi293 – 305Combined sources13
Beta strandi306 – 308Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti61E → Q (PubMed:6302686).Curated1
Sequence conflicti61E → Q AA sequence (PubMed:6341995).Curated1
Sequence conflicti87E → Q AA sequence (PubMed:6341995).Curated1
Sequence conflicti91D → N AA sequence (PubMed:6341995).Curated1
Sequence conflicti130D → N AA sequence (PubMed:6341995).Curated1
Sequence conflicti150Q → E in AAA24476 (PubMed:6364131).Curated1
Sequence conflicti196P → R in AAA97142 (PubMed:7610040).Curated1
Sequence conflicti221A → V (PubMed:6302686).Curated1
Sequence conflicti221A → V AA sequence (PubMed:6341995).Curated1
Sequence conflicti257N → D AA sequence (PubMed:6341995).Curated1
Sequence conflicti260 – 262ANM → MNA AA sequence (PubMed:6341995).Curated3
Sequence conflicti297R → L in AAA24474 (PubMed:6302686).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260722. 10 interactors.
DIPiDIP-35089N.
IntActiP0A786. 3 interactors.
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: November 2, 2016
This is version 117 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.