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purE from Brucella melitensis bv. 1 str. 16M

Victor ID 1215
Gene Name purE from Brucella melitensis bv. 1 str. 16M
Sequence Strain (Species/Organism) Brucella melitensis bv. 1 str. 16M
NCBI Gene ID 1196007
NCBI Protein GI 17986579
Locus Tag BMEI0296
Protein Accession NP_539213.1
Other Database IDs UniProtKB-ID: PURE_BRUME
UniRef100: UniRef100_P52558
UniRef90: UniRef90_P52558
UniRef50: UniRef50_Q5E1R4
UniParc: UPI0000132A6C
EMBL: U10241
EMBL: AE008917
EMBL-CDS: AAA57002.1
EMBL-CDS: AAL51477.1
RefSeq_NT: NC_003317.1
GenomeReviews: AE008917_GR
KEGG: bme:BMEI0296
HOGENOM: HBG301965
OMA: GVVMGSS
ProtClustDB: CLSK898071
BioCyc: BMEL224914:BMEI0296-MONOMER
Taxonomy ID 224914
Chromosome No I
Gene Starting Position 309338
Gene Ending Position 309880
Gene Strand (Orientation) -
Protein Name PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT
DNA Sequence 
>gi|17986284:309338-309880 Brucella melitensis bv. 1 str. 16M chromosome chromosome I, complete sequence
ATCAGGCTTCGTTCGAGGGGCGTTCTGCAACGCTTTCGGTCTGCGCCTTGCGCCATTCATCAAGACGGGC
GGCAAGTGCTTCATCATATAGCGCCAGAACGGCGGCGGCGAGAAGGGCGGCATTGACCGCGCCTGCACGG
CCGATGGCGAGAGTGCCGACGGGAATACCCGCTGGCATCTGTACGATGGAGAGTAGCGAATCCTGGCCCG
AAAGCGCCTTGGATTGAACTGGAACGCCAAAGACGGGAAGCGGTGTCATGGCAGCGGCCATGCCGGGCAG
GTGGGCCGCGCCGCCGGCGCCTGCGATGATGACCTTGAAGCCTTCCGCTTTCGCCCCCTTGGCGAAGGCG
ACCAGCCTGTCAGGGGTGCGATGGGCGGAAACGATCCGTGCGTCGAAGGAGATGCCGAGCGCCTCCAATG
TGTCGGCTGCATGGTGCATGGTTTCCCAATCGGACTGGCTTCCCATGATAATGGCGACATCAACGCTCAT
CGGTCTTTCCTGCTTGGCTTTTCGGTTGGCATGAGGAAGGTCTTGAAAAGACA
Protein Sequence 
>gi|17986579|ref|NP_539213.1| phosphoribosylaminoimidazole carboxylase catalytic subunit [Brucella melitensis bv. 1 str. 16M] MSFQDLPHANRKAKQERPMSVDVAIIMGSQSDWETMHHAADTLEALGISFDARIVSAHRTPDRLVAFAKGAKAEGFKVIIAGAGGAAHLPGMAAAMTPLPVFGVPVQSKALSGQDSLLSIVQMPAGIPVGTLAIGRAGAVNAALLAAAVLALYDEALAARLDEWRKAQTESVAERPSNEA
Molecule Role Virulence factor
Molecule Role Annotation FUNCTION: This subunit can alone transform AIR to CAIR, but in association with purK, which possesses an ATPase activity, an enzyme complex is produced which is capable of converting AIR to CAIR efficiently under physiological condition (By similarity)(UniProt: Q8FYW3).

CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2)(UniProt: Q8FYW3).

PATHWAY: Nucleotide biosynthesis; IMP biosynthesis; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 3(UniProt: Q8FYW3).

PATHWAY: Context: Purine biosynthesis(UniProt: Q8FYW3).

SUBUNIT: Homooctamer (By similarity)(UniProt: Q8FYW3).

SIMILARITY: Belongs to the AIR carboxylase family(UniProt: Q8FYW3).

MUTATION: Brucella abortus 2308 derivatives with mini-Tn5 insertions in purE, purL, and purD display significant attenuation in the BALBc mouse model. It confirms the importance of the purine biosynthesis pathways for the survival and replication of the brucellae in host macrophages (Alcantara et al., 2004). The purE mutant has reduced survival in murine macrophages and reduced virulence in mice (Alcantara et al., 2004).

A purE gene deletion mutant (purE201) of B melitensis was constructed as a potentially useful vaccine for humans and animals. At necropsy, bacteria were present in mammary lymph nodes or spleen of 33 of goats given virulent 16M but in none of goats given the purE mutant. The purE mutation of B melitensis 16M was stable and that the vaccine could be differentiated from wild-type strains by hybridization, purine auxotrophy, and kanamycin resistance. Mice clear the identical purE mutant strain from their spleens in only 8 weeks but remain infected with B. melitensis 16M for at least 3 months (Alcantara et al., 2004).
COG COG0041F, under F: Nucleotide transport and metabolism
References
Alcantara et al., 2004: Alcantara RB, Read RD, Valderas MW, Brown TD, Roop RM 2nd. Intact purine biosynthesis pathways are required for wild-type virulence of Brucella abortus 2308 in the BALB/c mouse model. Infection and immunity. 2004; 72(8); 4911-4917. [PubMed: 15271960].