P0A786 (PYRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pyrI	P0A7F3	12	EBI-906620,EBI-906630

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.11 Ref.12 Ref.13

Chain

2 – 311

310

Aspartate carbamoyltransferase catalytic chain HAMAP-Rule MF_00001

PRO_0000113128

Experimental info

Sequence conflict

61

1

E → Q Ref.1

Sequence conflict

61

1

E → Q AA sequence Ref.6

Sequence conflict

87

1

E → Q AA sequence Ref.6

Sequence conflict

91

1

D → N AA sequence Ref.6

Sequence conflict

130

1

D → N AA sequence Ref.6

Sequence conflict

150

1

Q → E in AAA24476. Ref.2

Sequence conflict

196

1

P → R in AAA97142. Ref.3

Sequence conflict

221

1

A → V Ref.1

Sequence conflict

221

1

A → V AA sequence Ref.6

Sequence conflict

257

1

N → D AA sequence Ref.6

Sequence conflict

260 – 262

3

ANM → MNA AA sequence Ref.6

Sequence conflict

297

1

R → L in AAA24474. Ref.1

Secondary structure

1

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311

Helix Strand Turn

Details...

Turn

4 – 7

4

Helix

13 – 15

3

Helix

18 – 33

16

Turn

37 – 42

6

Beta strand

44 – 51

8

Helix

54 – 65

12

Turn

66 – 68

3

Beta strand

70 – 75

6

Helix

77 – 79

3

Turn

80 – 82

3

Helix

86 – 96

11

Turn

97 – 99

3

Beta strand

101 – 109

9

Helix

112 – 119

8

Beta strand

120 – 122

3

Beta strand

125 – 130

6

Turn

131 – 133

3

Helix

136 – 150

15

Beta strand

153 – 155

3

Beta strand

157 – 162

6

Turn

164 – 166

3

Helix

168 – 178

11

Beta strand

180 – 182

3

Beta strand

184 – 188

5

Helix

191 – 193

3

Helix

197 – 205

9

Beta strand

210 – 212

3

Helix

216 – 218

3

Turn

219 – 222

4

Beta strand

224 – 228

5

Helix

233 – 235

3

Helix

238 – 244

7

Helix

245 – 247

3

Beta strand

248 – 250

3

Helix

252 – 255

4

Beta strand

256 – 258

3

Beta strand

263 – 265

3

Beta strand

271 – 274

4

Helix

276 – 279

4

Beta strand

281 – 284

4

Helix

286 – 291

6

Helix

293 – 305

13

Beta strand

306 – 308

3

Sequences

	Sequence		Length	Mass (Da)
	P0A786 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CC2F5ACBD73E0E3E	FASTA	311	34,427
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

PIR

DTECC. H65236.

RefSeq

NP_418666.1. NC_000913.2.
YP_492385.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ACM	X-ray	2.80	A/C	2-310	[»]
1AT1	X-ray	2.80	A/C	2-310	[»]
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	2-310	[»]
1F1B	X-ray	2.30	A/C	2-310	[»]
1GQ3	X-ray	2.01	A/B/C	2-311	[»]
1I5O	X-ray	2.80	A/C	2-310	[»]
1NBE	X-ray	2.60	A/C	2-310	[»]
1Q95	X-ray	2.46	A/B/C/D/E/F	2-310	[»]
1R0B	X-ray	2.90	A/B/C/D/E/F	2-310	[»]
1R0C	X-ray	2.37	A/G	2-310	[»]
1RAA	X-ray	2.50	A/C	2-310	[»]
1RAB	X-ray	2.50	A/C	2-310	[»]
1RAC	X-ray	2.50	A/C	2-310	[»]
1RAD	X-ray	2.50	A/C	2-310	[»]
1RAE	X-ray	2.50	A/C	2-310	[»]
1RAF	X-ray	2.50	A/C	2-310	[»]
1RAG	X-ray	2.50	A/C	2-310	[»]
1RAH	X-ray	2.50	A/C	2-310	[»]
1RAI	X-ray	2.50	A/C	2-310	[»]
1SKU	X-ray	2.60	A/C	2-310	[»]
1TTH	X-ray	2.80	A/C	2-310	[»]
1TU0	X-ray	2.55	A/C	2-310	[»]
1TUG	X-ray	2.10	A/C	2-310	[»]
1XJW	X-ray	2.71	A/C	2-310	[»]
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	2-310	[»]
2AIR	X-ray	2.00	A/G	2-310	[»]
2AT1	X-ray	2.80	A/C	2-310	[»]
2ATC	X-ray	3.00	A	2-310	[»]
2FZC	X-ray	2.10	A/C	2-310	[»]
2FZG	X-ray	2.25	A/C	2-310	[»]
2FZK	X-ray	2.50	A/C	2-310	[»]
2H3E	X-ray	2.30	A/C	2-310	[»]
2HSE	X-ray	2.60	A/C	2-310	[»]
2IPO	X-ray	2.60	A/C	2-310	[»]
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	2-310	[»]
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	2-310	[»]
9ATC	X-ray	2.40	A	2-310	[»]

ProteinModelPortal

P0A786.

SMR

P0A786. Positions 2-311.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A786. 3 interactions.

STRING

511145.b4245.

2D gel databases

SWISS-2DPAGE

P0A786.

Proteomic databases

PaxDb

P0A786.

PRIDE

P0A786.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77202; AAC77202; b4245.
BAE78244; BAE78244; BAE78244.

GeneID

12931728.
948767.

KEGG

ecj:Y75_p4130.
eco:b4245.

PATRIC

32124067. VBIEscCol129921_4378.

Organism-specific databases

EchoBASE

EB0798.

EcoGene

EG10805. pyrB.

Phylogenomic databases

eggNOG

COG0540.

HOGENOM

HOG000022685.

KO

K00609.

OMA

YGVPVRM.

ProtClustDB

PRK00856.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPCARBCAT-MONOMER.
ECOL316407:JW4204-MONOMER.
MetaCyc:ASPCARBCAT-MONOMER.

SABIO-RK

P0A786.

UniPathway

UPA00070; UER00116.

Gene expression databases

Genevestigator

P0A786.

Family and domain databases

HAMAP

MF_00001. Asp_carb_tr.

InterPro

IPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]

Pfam

PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]

PRINTS

PR00100. AOTCASE.
PR00101. ATCASE.

SUPFAM

SSF53671. Asp/Orn_carbamoyltranf. 1 hit.

TIGRFAMs

TIGR00670. asp_carb_tr. 1 hit.

PROSITE

PS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A786.

Entry information

Entry name

PYRB_ECOLI

Accession

Primary (citable) accession number: P0A786
Secondary accession number(s): P00479 , Q2M662, Q47555, Q47557

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program