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Q9WYS7 (PURE_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. 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 mutase
Short name=N5-CAIR mutase
EC=5.4.99.18
Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide mutase
Gene names
Name:purE
Ordered Locus Names:TM_0446
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length171 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.

Catalytic activity

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

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.

Subunit structure

Homooctamer. Ref.2

Sequence similarities

Belongs to the AIR carboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171N5-carboxyaminoimidazole ribonucleotide mutase
PRO_0000074980

Sites

Binding site101Substrate By similarity
Binding site131Substrate By similarity
Binding site401Substrate By similarity

Secondary structure

1 .......................... 171
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WYS7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 84A995A2E29B8E5F

FASTA17118,618
        10         20         30         40         50         60 
MPRVGIIMGS DSDLPVMKQA AEILEEFGID YEITIVSAHR TPDRMFEYAK NAEERGIEVI 

        70         80         90        100        110        120 
IAGAGGAAHL PGMVASITHL PVIGVPVKTS TLNGLDSLFS IVQMPGGVPV ATVAINNAKN 

       130        140        150        160        170 
AGILAASILG IKYPEIARKV KEYKERMKRE VLEKAQRLEQ IGYKEYLNQK E

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77-A resolution."
Schwarzenbacher R., Jaroszewski L., von Delft F., Abdubek P., Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Eshagi S., Floyd R., Godzik A., Grittini C. expand/collapse author list , Grzechnik S.K., Hampton E., Karlak C., Klock H.E., Koesema E., Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R., Quijano K., Robb A., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.
Proteins 55:474-478(2004) [PubMed: 15048837] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-171, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD35541.1.
PIRG72374.
RefSeqNP_228256.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O4VX-ray1.77A2-171[»]
ProteinModelPortalQ9WYS7.
SMRQ9WYS7. Positions 2-170.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID897464.
GenomeReviewsGene locus TM_0446 in contig AE000512_GR.
KEGGtma:TM0446.
NMPDRfig|243274.1.peg.440.
PATRIC23935777. VBITheMar51294_0452.
TIGRTM_0446.

Phylogenomic databases

HOGENOMHBG301965.
OMALIMGSDS.
PhylomeDBQ9WYS7.
ProtClustDBCLSK865332.

Enzyme and pathway databases

BioCycTMAR243274:TM_0446-MONOMER.

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.
KOK01588.
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 namePURE_THEMA
AccessionPrimary (citable) accession number: Q9WYS7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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