Reviewed, UniProtKB/Swiss-Prot P0AG18 (PUR6_ECOLI)

Names and origin

Protein names

Recommended name:
    Phosphoribosylaminoimidazole carboxylase catalytic subunit
    EC=4.1.1.21
Alternative name(s):
    AIR carboxylase
      Short name=AIRC

Gene names

Name:	purE
Ordered Locus Names:	b0523, JW0512

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	169 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	This subunit can alone transform AIR to CAIR, but in association with purK, which possesses an ATPase activity, an enzyme complex is produced which is capable of converting AIR to CAIR efficiently under physiological condition.
Catalytic activity	5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
Subunit structure	Homooctamer. Ref.7
Sequence similarities	Belongs to the AIR carboxylase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Decarboxylase Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	phosphoribosylaminoimidazole carboxylase activity Inferred from electronic annotation. Source: EC
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

Chain

2 – 169

168

Phosphoribosylaminoimidazole carboxylase catalytic subunit

PRO_0000074973

Sites

Binding site

16

1

Substrate

Binding site

19

1

Substrate

Binding site

46

1

Substrate

Secondary structure

1

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169

Helix Strand Turn

Details...

Beta strand

10 – 16

7

Helix

17 – 19

3

Helix

20 – 33

14

Beta strand

37 – 41

5

Turn

44 – 46

3

Helix

48 – 57

10

Turn

58 – 62

5

Beta strand

64 – 70

7

Helix

76 – 82

7

Beta strand

88 – 92

5

Turn

96 – 100

5

Helix

101 – 108

8

Helix

123 – 138

16

Helix

142 – 160

19

Sequences

	Sequence		Length	Mass (Da)
	P0AG18-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E8B745B8D86E7D0B	FASTA	169	17,780
	10 20 30 40 50 60 MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK LFSFAESAEE 70 80 90 100 110 120 NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA 130 140 150 160 IGKAGAANAA LLAAQILATH DKELHQRLND WRKAQTDEVL ENPDPRGAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence analysis of the purEK operon encoding 5'-phosphoribosyl-5-aminoimidazole carboxylase of Escherichia coli K-12." Tiedeman A.A., Keyhani J., Kamholz J., Daum H.A. III, Gots J.S., Smith J.M. J. Bacteriol. 171:205-212(1989) [PubMed: 2464576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis." Watanabe W., Sampei G., Aiba A., Mizobuchi K. J. Bacteriol. 171:198-204(1989) [PubMed: 2644189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases 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]. 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]	"Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway." Meyer E., Leonard N.J., Bhat B., Stubbe J., Smith J.M. Biochemistry 31:5022-5032(1992) [PubMed: 1534690] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 2-11.
[7]	"Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway." Mathews I.I., Kappock T.J., Stubbe J., Ealick S.E. Structure 7:1395-1406(1999) [PubMed: 10574791] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X12982 Genomic DNA. Translation: CAA31420.1.
M19657 Genomic DNA. Translation: AAA24449.1.
U82664 Genomic DNA. Translation: AAB40276.1.
U00096 Genomic DNA. Translation: AAC73625.1.
AP009048 Genomic DNA. Translation: BAE76300.1.

PIR

DEECPE. JT0499.

RefSeq

AP_001170.1.
NP_415056.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D7A	X-ray	2.50	A/B/C/D/L/M/N/O	8-167	[»]
1QCZ	X-ray	1.50	A	1-169	[»]
2ATE	X-ray	1.80	A	1-169	[»]
2NSH	X-ray	1.80	A	1-169	[»]
2NSJ	X-ray	2.31	A	1-169	[»]
2NSL	X-ray	2.00	A	1-169	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AG18.

2-D gel databases

SWISS-2DPAGE

P0AG18.

Genome annotation databases

GeneID

949031.

GenomeReviews

Gene locus JW0512 in contig AP009048_GR.
Gene locus b0523 in contig U00096_GR.

KEGG

ecj:JW0512.
eco:b0523.

Organism-specific databases

EchoBASE

EB0786.

EcoGene

EG10793. purE.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AG18.

OMA

GVVMGSS.

Enzyme and pathway databases

BioCyc

EcoCyc:PURE-MON.
MetaCyc:PURE-MON.

Gene expression databases

Genevestigator

P0AG18.

Family and domain databases

InterPro

IPR000031. AIR_COase_core.
[Graphical view]

Gene3D

G3DSA:3.40.50.7700. AIR_carboxyl. 1 hit.

PANTHER

PTHR23046. AIR_carboxyl. 1 hit.

Pfam

PF00731. AIRC. 1 hit.
[Graphical view]

ProDom

PD002193. AIR_carboxyl. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01162. purE. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PUR6_ECOLI

Accession

Primary (citable) accession number: P0AG18
Secondary accession number(s): P09028, Q2MBQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 39 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)