ID B7A6L6_THEAQ Unreviewed; 164 AA. AC B7A6L6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 11-DEC-2013, entry version 22. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase; DE Short=N5-CAIR mutase; DE EC=5.4.99.18; GN ORFNames=TaqDRAFT_4465; OS Thermus aquaticus Y51MC23. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=498848; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y51MC23; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., RA Brettin T.S., Mead D.; RT "Sequencing of the draft genome and assembly of Thermus aquaticus RT Y51MC23."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. 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. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ABVK02000002; EED10905.1; -; Genomic_DNA. DR EnsemblBacteria; EED10905; EED10905; TaqDRAFT_4465. DR PATRIC; 25940287; VBITheAqu66851_0560. DR UniPathway; UPA00074; UER00943. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-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; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR PIRSF; PIRSF001338; AIR_carboxylase; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. DR TIGRFAMs; TIGR01162; purE; 1. PE 3: Inferred from homology; KW 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 164 AA; 17064 MW; 1DCB892FA7E33D77 CRC64; MRPLVGVIMG SRSDWATMRH AAETLEALGV PYEVRVVSAH RTPDLMAEYA KTAEARGLMV IIAGAGGAAH LPGMTAAHTP LPVLGVPVES QALKGLDSLL SIVQMPAGVP VGTLAIGKAG AVNAALLAAS IVGLRHPEVM ERVKAYRRAQ TEAVLAHPDP REEA //