ID L3BSC5_ECOLX Unreviewed; 169 AA. AC L3BSC5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 26-FEB-2020, entry version 36. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}; DE Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}; DE EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929}; GN Name=purE {ECO:0000256|HAMAP-Rule:MF_01929}; GN ORFNames=A13W_04139 {ECO:0000313|EMBL:ELC91661.1}; OS Escherichia coli KTE193. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1181739 {ECO:0000313|EMBL:ELC91661.1, ECO:0000313|Proteomes:UP000010651}; RN [1] {ECO:0000313|EMBL:ELC91661.1, ECO:0000313|Proteomes:UP000010651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KTE193 {ECO:0000313|EMBL:ELC91661.1, RC ECO:0000313|Proteomes:UP000010651}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Escherichia coli KTE193."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide CC (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929, CC ECO:0000256|PIRNR:PIRNR001338}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate; CC Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730, CC ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. CC {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}. CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01929}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ELC91661.1}. 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; ANTH01000041; ELC91661.1; -; Genomic_DNA. DR RefSeq; WP_001295318.1; NZ_KB732454.1. DR SMR; L3BSC5; -. DR EnsemblBacteria; ELC91661; ELC91661; A13W_04139. DR PATRIC; fig|1181739.3.peg.4275; -. DR HOGENOM; CLU_094982_2_2_6; -. DR UniPathway; UPA00074; UER00943. DR Proteomes; UP000010651; Unassembled WGS sequence. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.7700; -; 1. DR HAMAP; MF_01929; PurE_classI; 1. DR InterPro; IPR033747; PurE_ClassI. DR InterPro; IPR000031; PurE_dom. DR InterPro; IPR024694; PurE_prokaryotes. DR InterPro; IPR035893; PurE_sf. 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 {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929, KW ECO:0000256|PIRNR:PIRNR001338}. FT DOMAIN 8..159 FT /note="AIRC" FT /evidence="ECO:0000259|SMART:SM01001" FT BINDING 16 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929, FT ECO:0000256|PIRSR:PIRSR001338-1" FT BINDING 19 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929, FT ECO:0000256|PIRSR:PIRSR001338-1" FT BINDING 46 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929, FT ECO:0000256|PIRSR:PIRSR001338-1" SQ SEQUENCE 169 AA; 17780 MW; E8B745B8D86E7D0B CRC64; MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK LFSFAESAEE NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA IGKAGAANAA LLAAQILATH DKELHQRLND WRKAQTDEVL ENPDPRGAA //