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P52559 (PURK_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N5-carboxyaminoimidazole ribonucleotide synthase

Short name=N5-CAIR synthase
EC=6.3.4.18
Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide synthetase
Gene names
Name:purK
Ordered Locus Names:BMEI0295
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

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 (N5-CAIR route): step 1/2.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the purK/purT family.

Contains 1 ATP-grasp domain.

Sequence caution

The sequence AAA57003.1 differs from that shown. Reason: Frameshift at positions 22, 43, 63, 67, 140 and 150.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362N5-carboxyaminoimidazole ribonucleotide synthase
PRO_0000074995

Regions

Domain112 – 300189ATP-grasp
Nucleotide binding185 – 1884ATP By similarity
Nucleotide binding270 – 2712ATP By similarity

Sites

Binding site1081ATP By similarity
Binding site1481ATP By similarity
Binding site1591ATP By similarity
Binding site1931ATP By similarity

Experimental info

Sequence conflict411Q → H Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52559 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 536A73DC33014F47

FASTA36238,682
        10         20         30         40         50         60 
MDKTSLKPGS TIGIIGGGQL GRMLAMAAAR FGYETIILEP QAGCPAAQVA NRQIVAAYDD 

        70         80         90        100        110        120 
PKALAELAAA SDVITYEFEN VPVSAADKLA ETALVLPPPA ALEISQDRFT EKQFLNESGI 

       130        140        150        160        170        180 
ETAPWRLVDD EETLIAALGA LGGRGILKIR RLGYDGKGQV RLASLDETQA CNAFAAINKA 

       190        200        210        220        230        240 
PAILEGFVEF EREVSVIAAR DRSGNVAIFD LAENVHKDGI LATSTVPAAI SVQTAEAART 

       250        260        270        280        290        300 
AAEKLLHALD YVGVLGLEFF VLKDGTLLAN EFAPRVHNSG HWTEAACAIS QFEQHIRAVA 

       310        320        330        340        350        360 
GLPLGNTDRH SDCVMENLIG DDIEKVPAIL CEKNAVLHLY GKKEARAGRK IGHVTRIKPR 


TI 

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References

« Hide 'large scale' references
[1]"Molecular cloning and genetic characterization of the purEK operon of Brucella melitensis strain 16M."
Warren R., Hoover D., Hadfield T., Drazek S.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 16M / ATCC 23456 / NCTC 10094.
[2]"The genome sequence of the facultative intracellular pathogen Brucella melitensis."
DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. expand/collapse author list , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R.
Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 16M / ATCC 23456 / NCTC 10094.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10241 Unassigned DNA. Translation: AAA57003.1. Frameshift.
AE008917 Genomic DNA. Translation: AAL51476.1.
PIRAI3288.
RefSeqNP_539212.1. NC_003317.1.

3D structure databases

ProteinModelPortalP52559.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1196006.
GenomeReviewsGene locus BMEI0295 in contig AE008917_GR.
KEGGbme:BMEI0295.
NMPDRfig|224914.1.peg.294.
PATRIC17802231. VBIBruMel146950_3432.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG516369.
OMAGRKMGHF.
PhylomeDBP52559.
ProtClustDBPRK06019.

Enzyme and pathway databases

BioCycBMEL224914:BMEI0295-MONOMER.

Family and domain databases

InterProIPR005875. AIR_COase_ATPase-su.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013816. ATP_grasp_subdomain_2.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KOK01589.
PfamPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMSSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.
TIGRFAMsTIGR01161. PurK. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURK_BRUME
AccessionPrimary (citable) accession number: P52559
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2002
Last modified: January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families