Reviewed, UniProtKB/Swiss-Prot P09029 (PURK_ECOLI)

Names and origin

Protein names

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

Gene names

Name:	purK
Ordered Locus Names:	b0522, JW0511

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Possesses an ATPase activity that is dependent on the presence of AIR (aminoimidazole ribonucleotide). The association of purK and purE produces an enzyme complex 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	Homodimer. Ref.7
Sequence similarities	Belongs to the purK/purT family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Nucleotide-binding
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
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Chain

1 – 355

355

Phosphoribosylaminoimidazole carboxylase ATPase subunit

PRO_0000074997

Regions

Domain

84 – 267

184

ATP-grasp

Nucleotide binding

153 – 156

4

ATP

Nucleotide binding

237 – 238

2

ATP

Sites

Binding site

80

1

ATP

Binding site

120

1

ATP

Binding site

131

1

ATP

Binding site

161

1

ATP

Experimental info

Sequence conflict

64 – 65

2

RH → PD in CAA31421. Ref.1

Secondary structure

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355

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

11 – 20

10

Helix

21 – 23

3

Beta strand

25 – 30

6

Turn

36 – 38

3

Helix

41 – 43

3

Beta strand

44 – 49

6

Helix

57 – 62

6

Turn

69 – 72

4

Helix

73 – 78

6

Helix

80 – 90

11

Beta strand

97 – 99

3

Turn

103 – 105

3

Helix

106 – 113

8

Beta strand

115 – 121

7

Beta strand

131 – 135

5

Helix

138 – 141

4

Helix

144 – 146

3

Turn

147 – 149

3

Beta strand

150 – 154

5

Beta strand

159 – 168

10

Beta strand

174 – 176

3

Beta strand

180 – 185

6

Beta strand

188 – 194

7

Helix

200 – 217

18

Beta strand

221 – 230

10

Beta strand

233 – 242

10

Helix

245 – 249

5

Helix

250 – 253

4

Beta strand

254 – 256

3

Helix

258 – 266

9

Beta strand

280 – 287

8

Helix

292 – 296

5

Beta strand

300 – 304

5

Beta strand

314 – 321

8

Helix

325 – 335

11

Helix

341 – 343

3

Helix

344 – 352

9

Sequences

	Sequence		Length	Mass (Da)
	P09029-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 93464E111E29AD9C	FASTA	355	39,461
	10 20 30 40 50 60 MKQVCVLGNG QLGRMLRQAG EPLGIAVWPV GLDAEPAAVP FQQSVITAEI ERWPETALTR 70 80 90 100 110 120 ELARHPAFVN RDVFPIIADR LTQKQLFDKL HLPTAPWQLL AERSEWPAVF DRLGELAIVK 130 140 150 160 170 180 RRTGGYDGRG QWRLRANETE QLPAECYGEC IVEQGINFSG EVSLVGARGF DGSTVFYPLT 190 200 210 220 230 240 HNLHQDGILR TSVAFPQANA QQQAQAEEML SAIMQELGYV GVMAMECFVT PQGLLINELA 250 260 270 280 290 300 PRVHNSGHWT QNGASISQFE LHLRAITDLP LPQPVVNNPS VMINLIGSDV NYDWLKLPLV 310 320 330 340 350 HLHWYDKEVR PGRKVGHLNL TDSDTSRLTA TLEALIPLLP PEYASGVIWA QSKFG

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 1-20.
[7]	"Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily." Thoden J.B., Kappock T.J., Stubbe J., Holden H.M. Biochemistry 38:15480-15492(1999) [PubMed: 10569930] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X12982 Genomic DNA. Translation: CAA31421.1.
M19657 Genomic DNA. Translation: AAA24450.1.
U82664 Genomic DNA. Translation: AAB40275.1.
U00096 Genomic DNA. Translation: AAC73624.1.
AP009048 Genomic DNA. Translation: BAE76299.1.

PIR

DCECPK. JU0001.

RefSeq

AP_001169.1.
NP_415055.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B6R	X-ray	2.10	A	1-355	[»]
1B6S	X-ray	2.50	A/B/C/D	1-355	[»]
3ETH	X-ray	1.60	A/B	1-355	[»]
3ETJ	X-ray	1.60	A/B	1-355	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P09029.

2-D gel databases

SWISS-2DPAGE

P09029.

Genome annotation databases

GeneID

945153.

GenomeReviews

Gene locus JW0511 in contig AP009048_GR.
Gene locus b0522 in contig U00096_GR.

KEGG

ecj:JW0511.
eco:b0522.

Organism-specific databases

EchoBASE

EB0789.

EcoGene

EG10796. purK.

CMR

Search...

Phylogenomic databases

HOGENOM

P09029.

OMA

KAMAVRI.

Enzyme and pathway databases

BioCyc

EcoCyc:PURK-MON.
MetaCyc:PURK-MON.

Gene expression databases

Genevestigator

P09029.

Family and domain databases

InterPro

IPR005875. AIR_COase_ATPase-su.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013816. ATP_grasp_subdomain_2.
IPR013817. Pre-ATP_grasp.
[Graphical view]

Gene3D

G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.

PANTHER

PTHR23047:SF1. PurK_ATP. 1 hit.

Pfam

PF02222. ATP-grasp. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01161. purK. 1 hit.

PROSITE

PS50975. ATP_GRASP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PURK_ECOLI

Accession

Primary (citable) accession number: P09029
Secondary accession number(s): Q2MBQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 94 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)