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Q2QJL3 (Q2QJL3_ACEAC) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 28. Feed History...

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

Protein namesRecommended name:
N5-carboxyaminoimidazole ribonucleotide mutase PIRNR PIRNR001338

Short name=N5-CAIR mutase PIRNR PIRNR001338
EC=5.4.99.18 PIRNR PIRNR001338
Gene names
Name:purE EMBL AAZ04483.1
OrganismAcetobacter aceti EMBL AAZ04483.1
Taxonomic identifier435 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) By similarity. PIRNR PIRNR001338

Catalytic activity

5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. PIRNR PIRNR001338

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 2/2. PIRNR PIRNR001338

Sequence similarities

Belongs to the AIR carboxylase family. PIRNR PIRNR001338

Sequences

Sequence LengthMass (Da)Tools
Q2QJL3 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: BA1F9245440138E8

FASTA18218,735
        10         20         30         40         50         60 
MSETAPLPSA SSALEDKAAS APVVGIIMGS QSDWETMRHA DALLTELEIP HETLIVSAHR 

        70         80         90        100        110        120 
TPDRLADYAR TAAERGLNVI IAGAGGAAHL PGMCAAWTRL PVLGVPVESR ALKGMDSLLS 

       130        140        150        160        170        180 
IVQMPGGVPV GTLAIGASGA KNAALLAASI LALYNPALAA RLETWRALQT ASVPNSPITE 


DK 

« Hide

References

[1]"Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti."
Constantine C.Z., Starks C.M., Mill C.P., Ransome A.E., Karpowicz S.J., Francois J.A., Goodman R.A., Kappock T.J.
Biochemistry 45:8193-8208(2006) [PubMed: 16819818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1023 EMBL AAZ04483.1.
[2]"Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE)."
Settembre E.C., Chittuluru J.R., Mill C.P., Kappock T.J., Ealick S.E.
Acta Crystallogr. D Biol. Crystallogr. 60:1753-1760(2004) [PubMed: 15388921] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ059549 Genomic DNA. Translation: AAZ04483.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U11X-ray1.55A/B1-182[»]
2FW1X-ray2.00A/B1-182[»]
2FW6X-ray1.85A/B1-182[»]
2FW7X-ray1.75A/B1-182[»]
2FW8X-ray1.75A/B1-182[»]
2FW9X-ray1.75A/B1-182[»]
2FWAX-ray1.90A/B1-182[»]
2FWBX-ray2.00A/B1-182[»]
2FWIX-ray1.94A/B1-182[»]
2FWJX-ray1.95A/B1-182[»]
2FWPX-ray1.85A/B1-182[»]
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024694. N5-CAIR_mutase_PurE.
IPR000031. N5-CAIR_Mutase_PurE_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.7700. AIR_carboxyl. 1 hit.
PfamPF00731. AIRC. 1 hit.
[Graphical view]
PIRSFPIRSF001338. AIR_carboxylase. 1 hit.
SMARTSM01001. AIRC. 1 hit.
[Graphical view]
SUPFAMSSF52255. AIR_carboxyl. 1 hit.
TIGRFAMsTIGR01162. PurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ2QJL3_ACEAC
AccessionPrimary (citable) accession number: Q2QJL3
Entry history
Integrated into UniProtKB/TrEMBL: January 24, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)