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Protein

N5-carboxyaminoimidazole ribonucleotide synthase

Gene

purK

Organism
Bacillus anthracis (strain A0248)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761ATP; via carbonyl oxygenCombined sources
Metal bindingi104 – 1041Magnesium 1; via carbonyl oxygenCombined sources
Binding sitei107 – 1071ADPCombined sources
Binding sitei107 – 1071ATP
Metal bindingi110 – 1101Magnesium 1Combined sources
Binding sitei147 – 1471ADPCombined sources
Binding sitei147 – 1471ATP
Binding sitei190 – 1901ADPCombined sources
Binding sitei190 – 1901ATP
Metal bindingi255 – 2551CalciumCombined sources
Metal bindingi255 – 2551Magnesium 2
Binding sitei255 – 2551ATP
Metal bindingi268 – 2681CalciumCombined sources
Metal bindingi268 – 2681Magnesium 2
Metal bindingi269 – 2691Magnesium 1; via carbonyl oxygenCombined sources
Binding sitei340 – 3401ATPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi153 – 1586ATP
Nucleotide bindingi154 – 1585ADPCombined sources
Nucleotide bindingi182 – 1854ADPCombined sources
Nucleotide bindingi182 – 1854ATP
Nucleotide bindingi213 – 2164ADPCombined sources
Nucleotide bindingi213 – 2164ATP
Nucleotide bindingi255 – 2573ADPCombined sources
Nucleotide bindingi267 – 2682ADPCombined sources
Nucleotide bindingi267 – 2682ATP
Nucleotide bindingi272 – 2754ATPCombined sources
Nucleotide bindingi347 – 3482ATPCombined sources

GO - Molecular functioni

  1. 5-(carboxyamino)imidazole ribonucleotide synthase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. NAD binding Source: InterPro
  5. phosphoribosylaminoimidazole carboxylase activity Source: InterPro

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: InterPro
  2. oxidation-reduction process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation, LyaseImported

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Keywords - Ligandi

ATP-bindingCombined sources, CalciumCombined sources, MagnesiumCombined sources, Metal-bindingCombined sources, Nucleotide-binding

Enzyme and pathway databases

BioCyciBANT592021:GJAQ-334-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N5-carboxyaminoimidazole ribonucleotide synthaseUniRule annotation (EC:6.3.4.18UniRule annotation)
Short name:
N5-CAIR synthaseUniRule annotation
Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide synthetaseUniRule annotation
Gene namesi
Name:purKImported
Ordered Locus Names:BAA_0344Imported
OrganismiBacillus anthracis (strain A0248)Imported
Taxonomic identifieri592021 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002335 Componenti: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi592021.BAA_0344.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q2OX-ray1.96A/B1-383[»]
3QFFX-ray1.96A/B1-383[»]
3R5HX-ray2.20A/B1-383[»]
3V4SX-ray2.02A/B1-378[»]
4DLKX-ray2.02A/B1-380[»]
ProteinModelPortaliC3PBM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PurK/PurT family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0026.
HOGENOMiHOG000034029.
KOiK01589.
OMAiDSPCGQV.
OrthoDBiEOG6QZMX7.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR005875. AIR_COase_ATPase-su.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006140. D-isomer_DH_NAD-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02826. 2-Hacid_dh_C. 1 hit.
PF02222. 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.

C3PBM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRIILPGKT IGIIGGGQLG RMMALAAKEM GYKIAVLDPT KNSPCAQVAD
60 70 80 90 100
IEIVASYDDL KAIQHLAEIS DVVTYEFENI DYRCLQWLEK HAYLPQGSQL
110 120 130 140 150
LSKTQNRFTE KNAIEKAGLP VATYRLVQNQ EQLTEAIAEL SYPSVLKTTT
160 170 180 190 200
GGYDGKGQVV LRSEADVDEA RKLANAAECI LEKWVPFEKE VSVIVIRSVS
210 220 230 240 250
GETKVFPVAE NIHVNNILHE SIVPARITEE LSQKAIAYAK VLADELELVG
260 270 280 290 300
TLAVEMFATA DGEIYINELA PRPHNSGHYT QDACETSQFG QHIRAICNLP
310 320 330 340 350
LGETNLLKPV VMVNILGEHI EGVLRQVNRL TGCYLHLYGK EEAKAQRKMG
360 370 380
HVNILNDNIE VALEKAKSLH IWDHQEQLLE GKR
Length:383
Mass (Da):42,517
Last modified:June 15, 2009 - v1
Checksum:iBE0E5E1A56F88287
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001598 Genomic DNA. Translation: ACQ48995.1.
RefSeqiYP_002864907.1. NC_012659.1.

Genome annotation databases

EnsemblBacteriaiACQ48995; ACQ48995; BAA_0344.
KEGGibai:BAA_0344.
PATRICi18766429. VBIBacAnt132916_0589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001598 Genomic DNA. Translation: ACQ48995.1.
RefSeqiYP_002864907.1. NC_012659.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q2OX-ray1.96A/B1-383[»]
3QFFX-ray1.96A/B1-383[»]
3R5HX-ray2.20A/B1-383[»]
3V4SX-ray2.02A/B1-378[»]
4DLKX-ray2.02A/B1-380[»]
ProteinModelPortaliC3PBM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi592021.BAA_0344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACQ48995; ACQ48995; BAA_0344.
KEGGibai:BAA_0344.
PATRICi18766429. VBIBacAnt132916_0589.

Phylogenomic databases

eggNOGiCOG0026.
HOGENOMiHOG000034029.
KOiK01589.
OMAiDSPCGQV.
OrthoDBiEOG6QZMX7.

Enzyme and pathway databases

BioCyciBANT592021:GJAQ-334-MONOMER.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR005875. AIR_COase_ATPase-su.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006140. D-isomer_DH_NAD-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02826. 2-Hacid_dh_C. 1 hit.
PF02222. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of Bacillus anthracis A0248."
    Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D., Brettin T.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A0248Imported.
  2. "Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis."
    Tuntland M.L., Johnson M.E., Fung L.W., Santarsiero B.D.
    Acta Crystallogr. D 67:870-874(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
  3. "Crystal Structure of purK: N5-carboxyaminoimidazole ribonucleotide synthetase."
    Fung L.W., Tuntland M.L., Santarsiero B.D., Johnson M.E.
    Submitted (FEB-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP.
  4. "Elucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis."
    Tuntland M.L., Santarsiero B.D., Johnson M.E., Fung L.W.
    Acta Crystallogr. D 70:3057-3065(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH ADP; ATP; CALCIUM AND MAGNESIUM.

Entry informationi

Entry nameiC3PBM5_BACAA
AccessioniPrimary (citable) accession number: C3PBM5
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2009
Last sequence update: June 15, 2009
Last modified: March 31, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

External Data

Dasty 3

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 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.