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 19-OCT-2011, entry version 79. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase; DE Short=N5-CAIR synthase; DE EC=6.3.4.18; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase; GN Name=purK; OrderedLocusNames=ML0735; ORFNames=B1308_F1_32; OS Mycobacterium leprae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96084954; PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8; RA Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I., RA Cole S.T., 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 MEDLINE=21128732; 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- CC aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR) (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole CC + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole. 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 1/2. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the purK/purT family. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. 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 ProteinModelPortal; P46701; -. DR EnsemblBacteria; EBMYCT00000028675; EBMYCP00000028281; EBMYCG00000028670. DR GeneID; 909683; -. DR GenomeReviews; AL450380_GR; ML0735. DR KEGG; mle:ML0735; -. DR NMPDR; fig|272631.1.peg.447; -. DR Leproma; ML0735; -. DR GeneTree; EBGT00050000015722; -. DR HOGENOM; HBG516369; -. DR OMA; GRKMGHF; -. DR ProtClustDB; PRK06019; -. DR BioCyc; MLEP272631:ML0735-MONOMER; -. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:EC. 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:InterPro. DR InterPro; IPR005875; AIR_COase_ATPase-su. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR013817; Pre-ATP_grasp. DR InterPro; IPR016185; PreATP-grasp-like. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1. DR Pfam; PF02222; ATP-grasp; 1. DR SUPFAM; SSF52440; PreATP-grasp-like; 1. DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1. DR TIGRFAMs; TIGR01161; PurK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Purine biosynthesis. FT CHAIN 1 439 N5-carboxyaminoimidazole ribonucleotide FT synthase. FT /FTId=PRO_0000074999. FT DOMAIN 117 313 ATP-grasp. FT NP_BIND 197 200 ATP (By similarity). FT NP_BIND 283 284 ATP (By similarity). FT BINDING 113 113 ATP (By similarity). FT BINDING 160 160 ATP (By similarity). FT BINDING 205 205 ATP (By similarity). 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 //