UniProtKB - P0A786 (PYRB_ECOLI)
Protein
Aspartate carbamoyltransferase catalytic subunit
Gene
pyrB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalytic activityi
- EC:2.1.3.2
: UMP biosynthesis via de novo pathway Pathwayi
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:
- Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA)
- Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase catalytic subunit (pyrB), Aspartate carbamoyltransferase (pyrB)
- Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC)
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
- amino acid binding Source: InterPro
- aspartate carbamoyltransferase activity Source: GO_Central
- identical protein binding Source: IntAct
GO - Biological processi
- 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
- 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
- cellular amino acid metabolic process Source: InterPro
- nitrogen compound metabolic process Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | Pyrimidine biosynthesis |
Enzyme and pathway databases
BioCyci | EcoCyc:ASPCARBCAT-MONOMER ECOL316407:JW4204-MONOMER MetaCyc:ASPCARBCAT-MONOMER |
BRENDAi | 2.1.3.2 2026 |
SABIO-RKi | P0A786 |
UniPathwayi | UPA00070;UER00116 |
Names & Taxonomyi
Protein namesi | Recommended name: Aspartate carbamoyltransferase catalytic subunit (EC:2.1.3.2)Alternative name(s): Aspartate transcarbamylase Short name: ATCase |
Gene namesi | Name:pyrB Ordered Locus Names:b4245, JW4204 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed4 Publications | |||
ChainiPRO_0000113128 | 2 – 311 | Aspartate carbamoyltransferase catalytic subunitAdd BLAST | 310 |
Proteomic databases
jPOSTi | P0A786 |
PaxDbi | P0A786 |
PRIDEi | P0A786 |
2D gel databases
SWISS-2DPAGEi | P0A786 |
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 PublicationBinary interactionsi
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGridi | 4260722, 54 interactors 853055, 1 interactor |
ComplexPortali | CPX-3091 Aspartate carbamoyltransferase complex |
DIPi | DIP-35089N |
IntActi | P0A786, 3 interactors |
MINTi | P0A786 |
STRINGi | 511145.b4245 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A786 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A786 |
Family & Domainsi
Sequence similaritiesi
Belongs to the ATCase/OTCase family.Curated
Phylogenomic databases
eggNOGi | ENOG4105CXT Bacteria COG0540 LUCA |
HOGENOMi | HOG000022685 |
InParanoidi | P0A786 |
KOi | K00609 |
PhylomeDBi | P0A786 |
Family and domain databases
Gene3Di | 3.40.50.1370, 2 hits |
HAMAPi | MF_00001 Asp_carb_tr, 1 hit |
InterProi | View protein in InterPro IPR006132 Asp/Orn_carbamoyltranf_P-bd IPR006130 Asp/Orn_carbamoylTrfase IPR036901 Asp/Orn_carbamoylTrfase_sf IPR002082 Asp_carbamoyltransf IPR006131 Asp_carbamoyltransf_Asp/Orn-bd |
PANTHERi | PTHR11405:SF16 PTHR11405:SF16, 1 hit |
Pfami | View protein in Pfam PF00185 OTCace, 1 hit PF02729 OTCace_N, 1 hit |
PRINTSi | PR00100 AOTCASE |
SUPFAMi | SSF53671 SSF53671, 1 hit |
TIGRFAMsi | TIGR00670 asp_carb_tr, 1 hit |
PROSITEi | View protein in PROSITE PS00097 CARBAMOYLTRANSFERASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A786-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 61 | E → Q in AAA24474 (PubMed:6302686).Curated | 1 | |
Sequence conflicti | 61 | E → Q AA sequence (PubMed:6341995).Curated | 1 | |
Sequence conflicti | 87 | E → Q AA sequence (PubMed:6341995).Curated | 1 | |
Sequence conflicti | 91 | D → N AA sequence (PubMed:6341995).Curated | 1 | |
Sequence conflicti | 130 | D → N AA sequence (PubMed:6341995).Curated | 1 | |
Sequence conflicti | 150 | Q → E in AAA24476 (PubMed:6364131).Curated | 1 | |
Sequence conflicti | 196 | P → R in AAA97142 (PubMed:7610040).Curated | 1 | |
Sequence conflicti | 221 | A → V in AAA24474 (PubMed:6302686).Curated | 1 | |
Sequence conflicti | 221 | A → V AA sequence (PubMed:6341995).Curated | 1 | |
Sequence conflicti | 257 | N → D AA sequence (PubMed:6341995).Curated | 1 | |
Sequence conflicti | 260 – 262 | ANM → MNA AA sequence (PubMed:6341995).Curated | 3 | |
Sequence conflicti | 297 | R → L in AAA24474 (PubMed:6302686).Curated | 1 |
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 WP_000013046.1, NZ_STEB01000013.1 |
Genome annotation databases
EnsemblBacteriai | AAC77202; AAC77202; b4245 BAE78244; BAE78244; BAE78244 |
GeneIDi | 948767 |
KEGGi | ecj:JW4204 eco:b4245 |
PATRICi | fig|1411691.4.peg.2456 |
Similar proteinsi
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 WP_000013046.1, NZ_STEB01000013.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
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 | 2-311 | [»] | |
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 | [»] | |
4WTO | X-ray | 2.03 | A/C | 2-311 | [»] | |
5AT1 | X-ray | 2.60 | A/C | 2-311 | [»] | |
5VMQ | X-ray | 2.01 | A/B/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 | [»] | |
SMRi | P0A786 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 4260722, 54 interactors 853055, 1 interactor |
ComplexPortali | CPX-3091 Aspartate carbamoyltransferase complex |
DIPi | DIP-35089N |
IntActi | P0A786, 3 interactors |
MINTi | P0A786 |
STRINGi | 511145.b4245 |
Chemistry databases
DrugBanki | DB05540 Alanosine |
2D gel databases
SWISS-2DPAGEi | P0A786 |
Proteomic databases
jPOSTi | P0A786 |
PaxDbi | P0A786 |
PRIDEi | P0A786 |
Genome annotation databases
EnsemblBacteriai | AAC77202; AAC77202; b4245 BAE78244; BAE78244; BAE78244 |
GeneIDi | 948767 |
KEGGi | ecj:JW4204 eco:b4245 |
PATRICi | fig|1411691.4.peg.2456 |
Organism-specific databases
EchoBASEi | EB0798 |
Phylogenomic databases
eggNOGi | ENOG4105CXT Bacteria COG0540 LUCA |
HOGENOMi | HOG000022685 |
InParanoidi | P0A786 |
KOi | K00609 |
PhylomeDBi | P0A786 |
Enzyme and pathway databases
UniPathwayi | UPA00070;UER00116 |
BioCyci | EcoCyc:ASPCARBCAT-MONOMER ECOL316407:JW4204-MONOMER MetaCyc:ASPCARBCAT-MONOMER |
BRENDAi | 2.1.3.2 2026 |
SABIO-RKi | P0A786 |
Miscellaneous databases
EvolutionaryTracei | P0A786 |
PROi | PR:P0A786 |
Family and domain databases
Gene3Di | 3.40.50.1370, 2 hits |
HAMAPi | MF_00001 Asp_carb_tr, 1 hit |
InterProi | View protein in InterPro IPR006132 Asp/Orn_carbamoyltranf_P-bd IPR006130 Asp/Orn_carbamoylTrfase IPR036901 Asp/Orn_carbamoylTrfase_sf IPR002082 Asp_carbamoyltransf IPR006131 Asp_carbamoyltransf_Asp/Orn-bd |
PANTHERi | PTHR11405:SF16 PTHR11405:SF16, 1 hit |
Pfami | View protein in Pfam PF00185 OTCace, 1 hit PF02729 OTCace_N, 1 hit |
PRINTSi | PR00100 AOTCASE |
SUPFAMi | SSF53671 SSF53671, 1 hit |
TIGRFAMsi | TIGR00670 asp_carb_tr, 1 hit |
PROSITEi | View protein in PROSITE PS00097 CARBAMOYLTRANSFERASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PYRB_ECOLI | |
Accessioni | P0A786Primary (citable) accession number: P0A786 Secondary accession number(s): P00479 Q47557 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | November 13, 2019 | |
This is version 141 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references