P0A7F3 (PYRI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate carbamoyltransferase regulatory chain

Gene names

Name:	pyrI
Ordered Locus Names:	b4244, JW4203

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	153 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)

Function	Involved in allosteric regulation of aspartate carbamoyltransferase. HAMAP-Rule MF_00002
Cofactor	Binds 1 zinc ion per subunit.
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.11
Sequence similarities	Belongs to the PyrI family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' pyrimidine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	aspartate carbamoyltransferase complex Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	zinc ion binding Inferred from direct assay PubMed 4550953. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pyrB	P0A786	12	EBI-906630,EBI-906620

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.6 Ref.8

Chain

2 – 153

152

Aspartate carbamoyltransferase regulatory chain HAMAP-Rule MF_00002

PRO_0000142303

Sites

Metal binding

109

1

Zinc

Metal binding

114

1

Zinc

Metal binding

138

1

Zinc

Metal binding

141

1

Zinc

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

153

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Beta strand

13 – 21

9

Turn

23 – 25

3

Helix

26 – 32

7

Turn

33 – 36

4

Beta strand

37 – 40

4

Beta strand

42 – 50

9

Turn

51 – 53

3

Beta strand

54 – 62

9

Helix

68 – 72

5

Turn

73 – 77

5

Beta strand

78 – 80

3

Beta strand

82 – 87

6

Beta strand

90 – 95

6

Beta strand

101 – 106

6

Beta strand

112 – 114

3

Turn

115 – 118

4

Beta strand

119 – 121

3

Beta strand

124 – 129

6

Beta strand

131 – 138

8

Turn

139 – 141

3

Beta strand

144 – 146

3

Helix

147 – 152

6

Sequences

	Sequence		Length	Mass (Da)
	P0A7F3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 81A1631614E549EA	FASTA	153	17,121
	10 20 30 40 50 60 MTHDNKLQVE AIKRGTVIDH IPAQIGFKLL SLFKLTETDQ RITIGLNLPS GEMGRKDLIK 70 80 90 100 110 120 IENTFLSEDQ VDQLALYAPQ ATVNRIDNYE VVGKSRPSLP ERIDNVLVCP NSNCISHAEP 130 140 150 VSSSFAVRKR ANDIALKCKY CEKEFSHNVV LAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"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.
[3]	"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]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	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 2-11. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"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 2-13. Strain: K12 / EMG2.
[7]	"Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. I. Primary structure of a pyrI gene encoding a modified regulatory subunit." Cunin R., Jacobs A., Charlier D.R.M., Crabeel M., Herve G., Glansdorff N., Pierard A. J. Mol. Biol. 186:707-713(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-153.
[8]	"New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain." Weber K. Nature 218:1116-1119(1968) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-153.
[9]	"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.
[10]	"Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate." Monaco H.L., Crawford J.L., Lipscomb W.N. Proc. Natl. Acad. Sci. U.S.A. 75:5276-5280(1978) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[11]	"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.
[12]	"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).
[13]	"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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K01472 Genomic DNA. Translation: AAA24477.1.
U14003 Genomic DNA. Translation: AAA97141.1.
U00096 Genomic DNA. Translation: AAC77201.1.
AP009048 Genomic DNA. Translation: BAE78243.1.
M28578 Genomic DNA. Translation: AAA24487.1.

PIR

DTECR. A93985.

RefSeq

NP_418665.1. NC_000913.2.
YP_492384.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ACM	X-ray	2.80	B/D	2-152	[»]
1AT1	X-ray	2.80	B/D	2-152	[»]
1D09	X-ray	2.10	B/D	1-153	[»]
1EZZ	X-ray	2.70	B/D	1-153	[»]
1F1B	X-ray	2.30	B/D	1-153	[»]
1I5O	X-ray	2.80	B/D	1-153	[»]
1NBE	X-ray	2.60	B/D	2-152	[»]
1Q95	X-ray	2.46	G/H/I/J/K/L	1-152	[»]
1R0B	X-ray	2.90	G/H/I/J/K/L	1-152	[»]
1R0C	X-ray	2.37	B/H	1-152	[»]
1RAA	X-ray	2.50	B/D	2-152	[»]
1RAB	X-ray	2.50	B/D	2-152	[»]
1RAC	X-ray	2.50	B/D	2-152	[»]
1RAD	X-ray	2.50	B/D	2-152	[»]
1RAE	X-ray	2.50	B/D	2-152	[»]
1RAF	X-ray	2.50	B/D	2-152	[»]
1RAG	X-ray	2.50	B/D	2-152	[»]
1RAH	X-ray	2.50	B/D	2-152	[»]
1RAI	X-ray	2.50	B/D	2-152	[»]
1SKU	X-ray	2.60	B/D	1-152	[»]
1TTH	X-ray	2.80	B/D	2-152	[»]
1TU0	X-ray	2.55	B/D	2-152	[»]
1TUG	X-ray	2.10	B/D	2-152	[»]
1XJW	X-ray	2.71	B/D	2-152	[»]
1ZA1	X-ray	2.20	B/D	1-153	[»]
1ZA2	X-ray	2.50	B/D	1-153	[»]
2A0F	X-ray	2.90	B/D	2-152	[»]
2AIR	X-ray	2.00	B/H	1-153	[»]
2AT1	X-ray	2.80	B/D	2-152	[»]
2ATC	X-ray	3.00	B	6-152	[»]
2FZC	X-ray	2.10	B/D	1-152	[»]
2FZG	X-ray	2.25	B/D	1-152	[»]
2FZK	X-ray	2.50	B/D	1-152	[»]
2H3E	X-ray	2.30	B/D	1-152	[»]
2HSE	X-ray	2.60	B/D	2-152	[»]
2IPO	X-ray	2.60	B/D	2-152	[»]
2QG9	X-ray	2.70	B/D	1-153	[»]
2QGF	X-ray	2.20	B/D	1-153	[»]
3AT1	X-ray	2.80	B/D	2-152	[»]
3D7S	X-ray	2.80	B/D	1-153	[»]
3MPU	X-ray	2.86	B/D/F	1-153	[»]
4AT1	X-ray	2.60	B/D	1-153	[»]
4E2F	X-ray	2.80	B/D/F/H/J/L	1-153	[»]
4F04	X-ray	2.30	B/D	1-153	[»]
4FYV	X-ray	2.10	B/D	1-153	[»]
4FYW	X-ray	2.10	B/D	1-153	[»]
4FYX	X-ray	2.09	B/D	1-153	[»]
4FYY	X-ray	1.94	B/D	1-153	[»]
5AT1	X-ray	2.60	B/D	1-153	[»]
6AT1	X-ray	2.60	B/D	1-153	[»]
7AT1	X-ray	2.80	B/D	1-153	[»]
8AT1	X-ray	2.80	B/D	1-153	[»]
8ATC	X-ray	2.50	B/D	2-152	[»]
9ATC	X-ray	2.40	B	8-152	[»]

ProteinModelPortal

P0A7F3.

SMR

P0A7F3. Positions 6-153.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7F3. 2 interactions.

MINT

MINT-1541364.

STRING

511145.b4244.

2D gel databases

SWISS-2DPAGE

P0A7F3.

Proteomic databases

PaxDb

P0A7F3.

PRIDE

P0A7F3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77201; AAC77201; b4244.
BAE78243; BAE78243; BAE78243.

GeneID

12934123.
948763.

KEGG

ecj:Y75_p4129.
eco:b4244.

PATRIC

32124065. VBIEscCol129921_4377.

Organism-specific databases

EchoBASE

EB0804.

EcoGene

EG10811. pyrI.

Phylogenomic databases

eggNOG

COG1781.

HOGENOM

HOG000113530.

KO

K00610.

OMA

TVIDHIT.

ProtClustDB

PRK00893.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPCARBREG-MONOMER.
ECOL316407:JW4203-MONOMER.
MetaCyc:ASPCARBREG-MONOMER.

Gene expression databases

Genevestigator

P0A7F3.

Family and domain databases

Gene3D

2.30.30.20. 1 hit.
3.30.70.140. 1 hit.

HAMAP

MF_00002. Asp_carb_tr_reg.

InterPro

IPR020545. Asp_carbamoyltransf_reg_N.
IPR002801. Asp_carbamoylTrfase_reg.
IPR020542. Asp_carbamoyltrfase_reg_C.
[Graphical view]

Pfam

PF01948. PyrI. 1 hit.
PF02748. PyrI_C. 1 hit.
[Graphical view]

ProDom

PD006194. Asp_carbamoylTrfase_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54893. Asp_carbamoylTrfase_reg. 1 hit.
SSF57825. Asp_transf_reg_C. 1 hit.

TIGRFAMs

TIGR00240. ATCase_reg. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7F3.

Entry information

Entry name

PYRI_ECOLI

Accession

Primary (citable) accession number: P0A7F3
Secondary accession number(s): P00478, Q2M663

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program