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Protein

N5-carboxyaminoimidazole ribonucleotide synthase

Gene

purK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO3- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).UniRule annotation1 Publication

Catalytic activityi

ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3- = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole.UniRule annotation1 Publication

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route).UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. N5-carboxyaminoimidazole ribonucleotide synthase (purK)
  2. N5-carboxyaminoimidazole ribonucleotide mutase (purE)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80ATPUniRule annotation2 Publications1
Binding sitei120ATPUniRule annotation2 Publications1
Binding sitei161ATPUniRule annotation2 Publications1
Binding sitei184ATPUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi125 – 131ATPUniRule annotation2 Publications7
Nucleotide bindingi153 – 156ATPUniRule annotation2 Publications4
Nucleotide bindingi237 – 238ATPUniRule annotation2 Publications2

GO - Molecular functioni

  • 5-(carboxyamino)imidazole ribonucleotide synthase activity Source: EcoCyc
  • ATP binding Source: EcoCyc
  • metal ion binding Source: InterPro
  • phosphoribosylaminoimidazole carboxylase activity Source: EcoliWiki
  • phosphoribosylaminoimidazolesuccinocarboxamide synthase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PURK-MONOMER.
ECOL316407:JW0511-MONOMER.
MetaCyc:PURK-MONOMER.
BRENDAi6.3.4.18. 2026.
UniPathwayiUPA00074; UER00942.

Names & Taxonomyi

Protein namesi
Recommended name:
N5-carboxyaminoimidazole ribonucleotide synthaseUniRule annotationCurated (EC:6.3.4.18UniRule annotation1 Publication)
Short name:
N5-CAIR synthaseUniRule annotationCurated
Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide synthetaseUniRule annotationCurated
Gene namesi
Name:purKUniRule annotation
Ordered Locus Names:b0522Imported, JW0511Imported
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10796. purK.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000749971 – 355N5-carboxyaminoimidazole ribonucleotide synthaseAdd BLAST355

Proteomic databases

PaxDbiP09029.
PRIDEiP09029.

2D gel databases

SWISS-2DPAGEP09029.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4259875. 16 interactors.
IntActiP09029. 5 interactors.
STRINGi511145.b0522.

Structurei

Secondary structure

1355
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi11 – 20Combined sources10
Helixi21 – 23Combined sources3
Beta strandi26 – 30Combined sources5
Helixi36 – 38Combined sources3
Helixi41 – 43Combined sources3
Beta strandi44 – 49Combined sources6
Helixi57 – 63Combined sources7
Turni69 – 72Combined sources4
Helixi73 – 78Combined sources6
Helixi80 – 89Combined sources10
Beta strandi97 – 100Combined sources4
Helixi103 – 105Combined sources3
Helixi106 – 113Combined sources8
Beta strandi115 – 124Combined sources10
Turni127 – 130Combined sources4
Beta strandi131 – 135Combined sources5
Turni136 – 138Combined sources3
Helixi139 – 141Combined sources3
Helixi144 – 146Combined sources3
Turni147 – 149Combined sources3
Beta strandi150 – 154Combined sources5
Beta strandi159 – 168Combined sources10
Beta strandi174 – 176Combined sources3
Beta strandi180 – 185Combined sources6
Beta strandi188 – 194Combined sources7
Helixi200 – 217Combined sources18
Beta strandi221 – 230Combined sources10
Beta strandi233 – 242Combined sources10
Helixi245 – 249Combined sources5
Helixi250 – 253Combined sources4
Beta strandi254 – 256Combined sources3
Helixi258 – 266Combined sources9
Beta strandi280 – 287Combined sources8
Helixi292 – 296Combined sources5
Beta strandi301 – 304Combined sources4
Beta strandi314 – 321Combined sources8
Helixi325 – 335Combined sources11
Helixi336 – 338Combined sources3
Helixi341 – 343Combined sources3
Helixi344 – 353Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B6RX-ray2.10A1-355[»]
1B6SX-ray2.50A/B/C/D1-355[»]
3ETHX-ray1.60A/B1-355[»]
3ETJX-ray1.60A/B1-355[»]
ProteinModelPortaliP09029.
SMRiP09029.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09029.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini84 – 267ATP-graspUniRule annotationAdd BLAST184

Sequence similaritiesi

Belongs to the PurK/PurT family.UniRule annotationCurated
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CY8. Bacteria.
COG0026. LUCA.
HOGENOMiHOG000034026.
InParanoidiP09029.
KOiK01589.
OMAiCHIHWYG.
PhylomeDBiP09029.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_01928. PurK. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR005875. PurK.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01161. purK. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQVCVLGNG QLGRMLRQAG EPLGIAVWPV GLDAEPAAVP FQQSVITAEI
60 70 80 90 100
ERWPETALTR ELARHPAFVN RDVFPIIADR LTQKQLFDKL HLPTAPWQLL
110 120 130 140 150
AERSEWPAVF DRLGELAIVK RRTGGYDGRG QWRLRANETE QLPAECYGEC
160 170 180 190 200
IVEQGINFSG EVSLVGARGF DGSTVFYPLT HNLHQDGILR TSVAFPQANA
210 220 230 240 250
QQQAQAEEML SAIMQELGYV GVMAMECFVT PQGLLINELA PRVHNSGHWT
260 270 280 290 300
QNGASISQFE LHLRAITDLP LPQPVVNNPS VMINLIGSDV NYDWLKLPLV
310 320 330 340 350
HLHWYDKEVR PGRKVGHLNL TDSDTSRLTA TLEALIPLLP PEYASGVIWA

QSKFG
Length:355
Mass (Da):39,461
Last modified:November 1, 1997 - v2
Checksum:i93464E111E29AD9C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64 – 65RH → PD in CAA31421 (PubMed:2464576).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJU0001. DCECPK.
RefSeqiNP_415055.1. NC_000913.3.
WP_000815571.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73624; AAC73624; b0522.
BAE76299; BAE76299; BAE76299.
GeneIDi945153.
KEGGiecj:JW0511.
eco:b0522.
PATRICi32116204. VBIEscCol129921_0543.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJU0001. DCECPK.
RefSeqiNP_415055.1. NC_000913.3.
WP_000815571.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B6RX-ray2.10A1-355[»]
1B6SX-ray2.50A/B/C/D1-355[»]
3ETHX-ray1.60A/B1-355[»]
3ETJX-ray1.60A/B1-355[»]
ProteinModelPortaliP09029.
SMRiP09029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259875. 16 interactors.
IntActiP09029. 5 interactors.
STRINGi511145.b0522.

2D gel databases

SWISS-2DPAGEP09029.

Proteomic databases

PaxDbiP09029.
PRIDEiP09029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73624; AAC73624; b0522.
BAE76299; BAE76299; BAE76299.
GeneIDi945153.
KEGGiecj:JW0511.
eco:b0522.
PATRICi32116204. VBIEscCol129921_0543.

Organism-specific databases

EchoBASEiEB0789.
EcoGeneiEG10796. purK.

Phylogenomic databases

eggNOGiENOG4105CY8. Bacteria.
COG0026. LUCA.
HOGENOMiHOG000034026.
InParanoidiP09029.
KOiK01589.
OMAiCHIHWYG.
PhylomeDBiP09029.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00942.
BioCyciEcoCyc:PURK-MONOMER.
ECOL316407:JW0511-MONOMER.
MetaCyc:PURK-MONOMER.
BRENDAi6.3.4.18. 2026.

Miscellaneous databases

EvolutionaryTraceiP09029.
PROiP09029.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_01928. PurK. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR005875. PurK.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01161. purK. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPURK_ECOLI
AccessioniPrimary (citable) accession number: P09029
Secondary accession number(s): Q2MBQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be the ATPase subunit of phosphoribosylaminoimidazole carboxylase, with catalytic subunit PurE.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.