Reviewed, UniProtKB/Swiss-Prot P0A786 (PYRB_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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 MF_00001
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6. HAMAP 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.14
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
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro amino acid metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from direct assay. 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...

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 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

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311

Helix Strand Turn

Details...

Turn

4 – 7

4

Helix

18 – 33

16

Turn

37 – 42

6

Beta strand

44 – 51

8

Helix

55 – 66

12

Beta strand

70 – 75

6

Helix

77 – 79

3

Helix

81 – 84

4

Helix

89 – 96

8

Turn

97 – 99

3

Beta strand

101 – 110

10

Helix

112 – 115

4

Turn

116 – 119

4

Beta strand

125 – 130

6

Helix

136 – 150

15

Beta strand

153 – 155

3

Beta strand

157 – 162

6

Helix

168 – 177

10

Beta strand

180 – 182

3

Beta strand

184 – 188

5

Helix

191 – 193

3

Helix

197 – 205

9

Beta strand

209 – 212

4

Helix

216 – 218

3

Turn

219 – 221

3

Beta strand

224 – 228

5

Turn

233 – 235

3

Helix

238 – 243

6

Helix

252 – 254

3

Beta strand

255 – 257

3

Beta strand

263 – 265

3

Beta strand

271 – 274

4

Helix

276 – 280

5

Helix

286 – 291

6

Helix

293 – 305

13

Sequences

	Sequence		Length	Mass (Da)
	P0A786-1 [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: 6302686] [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: 6364131] [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: 7610040] [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: 9278503] [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: 16738553] [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: 6341995] [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: 2459698] [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: 3928602] [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: 6300835] [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: 1699940] [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: 9298646] [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: 9629924] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[14]	"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: 6377306] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
[15]	"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: 2271528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[16]	"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: 2271529] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[17]	"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: 10318893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_004743.1.
NP_418666.1.

3D structure databases

PDBPDBe

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	1-311	[»]
1ZA2	X-ray	2.50	A/C	1-311	[»]
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	[»]
4AT1	X-ray	2.60	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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A786. 3 interactions.

2-D gel databases

SWISS-2DPAGE

P0A786.

ECO2DBASE

H031.3. 6TH EDITION.

Genome annotation databases

GeneID

948767.

GenomeReviews

Gene locus JW4204 in contig AP009048_GR.
Gene locus b4245 in contig U00096_GR.

KEGG

ecj:JW4204.
eco:b4245.

Organism-specific databases

EchoBASE

EB0798.

EcoGene

EG10805. pyrB.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A786.

OMA

P0A786. LYTIREN.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPCARBCAT-MON.
MetaCyc:ASPCARBCAT-MON.

Family and domain databases

HAMAP

MF_00001.
[Tree]

InterPro

IPR006132. Asp/Orn_carbamoyltranf_P_bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082. Aspartate_carbamoyltransf_euk.
[Graphical view]

Pfam

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

PRINTS

PR00100. AOTCASE.
PR00101. ATCASE.

TIGRFAMs

TIGR00670. asp_carb_tr. 1 hit.

PROSITE

PS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)