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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801ATPUniRule annotation2 Publications
Binding sitei120 – 1201ATPUniRule annotation2 Publications
Binding sitei161 – 1611ATPUniRule annotation2 Publications
Binding sitei184 – 1841ATPUniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi125 – 1317ATPUniRule annotation2 Publications
Nucleotide bindingi153 – 1564ATPUniRule annotation2 Publications
Nucleotide bindingi237 – 2382ATPUniRule annotation2 Publications

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355N5-carboxyaminoimidazole ribonucleotide synthasePRO_0000074997Add
BLAST

Proteomic databases

PaxDbiP09029.
PRIDEiP09029.

2D gel databases

SWISS-2DPAGEP09029.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4259875. 16 interactions.
IntActiP09029. 5 interactions.
STRINGi511145.b0522.

Structurei

Secondary structure

1
355
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi11 – 2010Combined sources
Helixi21 – 233Combined sources
Beta strandi26 – 305Combined sources
Helixi36 – 383Combined sources
Helixi41 – 433Combined sources
Beta strandi44 – 496Combined sources
Helixi57 – 637Combined sources
Turni69 – 724Combined sources
Helixi73 – 786Combined sources
Helixi80 – 8910Combined sources
Beta strandi97 – 1004Combined sources
Helixi103 – 1053Combined sources
Helixi106 – 1138Combined sources
Beta strandi115 – 12410Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1355Combined sources
Turni136 – 1383Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 1463Combined sources
Turni147 – 1493Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi188 – 1947Combined sources
Helixi200 – 21718Combined sources
Beta strandi221 – 23010Combined sources
Beta strandi233 – 24210Combined sources
Helixi245 – 2495Combined sources
Helixi250 – 2534Combined sources
Beta strandi254 – 2563Combined sources
Helixi258 – 2669Combined sources
Beta strandi280 – 2878Combined sources
Helixi292 – 2965Combined sources
Beta strandi301 – 3044Combined sources
Beta strandi314 – 3218Combined sources
Helixi325 – 33511Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 35310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-355.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09029.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 267184ATP-graspUniRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 652RH → PD in CAA31421 (PubMed:2464576).Curated

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
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. Positions 1-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259875. 16 interactions.
IntActiP09029. 5 interactions.
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: September 7, 2016
This is version 147 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.