ID A8FAM1_BACP2 Unreviewed; 162 AA.
AC A8FAM1;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 29-MAY-2013, entry version 40.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase;
DE Short=N5-CAIR mutase;
DE EC=5.4.99.18;
GN Name=purE; OrderedLocusNames=BPUM_0596;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C.,
RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.,
RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M.,
RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P.,
RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D.,
RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E.,
RA Venkateswaran K., Highlander S.K., Weinstock G.M.;
RT "Paradoxical DNA Repair and Peroxide Resistance Gene Conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole
CC ribonucleotide (CAIR) (By similarity).
CC -!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D-
CC ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxylate.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family.
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DR EMBL; CP000813; ABV61288.1; -; Genomic_DNA.
DR RefSeq; YP_001485848.1; NC_009848.1.
DR ProteinModelPortal; A8FAM1; -.
DR SMR; A8FAM1; 1-156.
DR STRING; 315750.BPUM_0596; -.
DR EnsemblBacteria; ABV61288; ABV61288; BPUM_0596.
DR GeneID; 5619844; -.
DR KEGG; bpu:BPUM_0596; -.
DR PATRIC; 18964975; VBIBacPum16546_0605.
DR eggNOG; COG0041; -.
DR HOGENOM; HOG000034140; -.
DR KO; K01588; -.
DR OMA; QSDWATM; -.
DR ProtClustDB; CLSK886818; -.
DR BioCyc; BPUM315750:GH6N-634-MONOMER; -.
DR UniPathway; UPA00074; UER00943.
DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.7700; -; 1.
DR InterPro; IPR024694; N5-CAIR_mutase_PurE.
DR InterPro; IPR000031; N5-CAIR_Mutase_PurE_dom.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF52255; AIR_carboxyl; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isomerase; Lyase; Purine biosynthesis.
FT BINDING 11 11 Substrate (By similarity).
FT BINDING 14 14 Substrate (By similarity).
FT BINDING 41 41 Substrate (By similarity).
SQ SEQUENCE 162 AA; 16928 MW; 1FC7A6A959C11B1A CRC64;
MKPLVGVIMG STSDWETMKN ACDILEELDI PYEKQVVSAH RTPDLMFEYA TEARGKGLKV
IIAGAGGAAH LPGMVAAKTT LPVIGVPVQS KALNGLDSLL SIVQMPGGVP VATVAIGKAG
ATNAGLLAAQ MISAFDETIA ARLEKRREQT KQTVLESSDQ LG
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