ID PURK_MYCLE Reviewed; 439 AA. AC P46701; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 23-FEB-2022, entry version 125. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928}; DE Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928}; DE EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928}; GN Name=purK {ECO:0000255|HAMAP-Rule:MF_01928}; OrderedLocusNames=ML0735; GN ORFNames=B1308_F1_32; OS Mycobacterium leprae (strain TN). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=272631; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8; RA Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I., Cole S.T., RA Smith D.R., Smith I.; RT "Genomic organization of the mycobacterial sigma gene cluster."; RL Gene 165:67-70(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole CC ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR). {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + CC hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + CC ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; CC EC=6.3.4.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01928}; 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 1/2. CC {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP- CC Rule:MF_01928}. 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; U00012; AAA85935.1; -; Genomic_DNA. DR EMBL; AL583919; CAC30244.1; -; Genomic_DNA. DR PIR; H87000; H87000. DR RefSeq; NP_301575.1; NC_002677.1. DR RefSeq; WP_010907899.1; NC_002677.1. DR SMR; P46701; -. DR STRING; 272631.ML0735; -. DR EnsemblBacteria; CAC30244; CAC30244; CAC30244. DR KEGG; mle:ML0735; -. DR PATRIC; fig|272631.5.peg.1332; -. DR Leproma; ML0735; -. DR eggNOG; COG0026; Bacteria. DR HOGENOM; CLU_011534_0_2_11; -. DR OMA; ITFDHEH; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000806; Chromosome. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1490.20; -; 1. DR HAMAP; MF_01928; PurK; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR005875; PurK. DR InterPro; IPR040686; PurK_C. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02222; ATP-grasp; 1. DR Pfam; PF17769; PurK_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01161; purK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1..439 FT /note="N5-carboxyaminoimidazole ribonucleotide synthase" FT /id="PRO_0000074999" FT DOMAIN 117..313 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928" FT NP_BIND 197..200 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928" FT NP_BIND 283..284 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928" FT BINDING 113 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928" FT BINDING 160 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928" FT BINDING 205 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928" SQ SEQUENCE 439 AA; 47306 MW; 288C5DD5EE7508EE CRC64; MMAVPSRCSL GVAPLVAMVG GGQLARMTHQ AAIALGQTLR VLATAADEPA AQVTPDVVIG SHTDLEDLRR VALGADALTF DHEHVPTELL DKLVAEGINV APSPQALVHA QDKLVMRRRL AALGAAMPRF MALDSVDDLA EIDAFAQRLT GSKDAPMVVK AVRGGYDGRG VQMVRDSAHA REVASGYLVD GMPVLVEERV ELRRELSALV ARSPFGQGAA WPVVETVQRD GICVLVVAPA LALADDLASA AQQLALRLAA ELGVVGVFAV ELFETADGAL LVNELAMRPH NSGHWTMDGA RTSQFEQHLR AVLDYPLGET DAVAPVTVMV NVLGAPQPPT LSVVTMDERL HHLFARMPDA RVHLYDKVER PGRKVGHINF RGTDKDRKNP TKLRERAELA AHWLSHGQWT DGWDPHRAGD DVVEISLACG GRNDAQRQR //