ID A0PRI7_MYCUA Unreviewed; 424 AA. AC A0PRI7; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 10-JUN-2026, entry version 109. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; GN Name=purK {ECO:0000256|HAMAP-Rule:MF_01928, GN ECO:0000256|RuleBase:RU361200, ECO:0000313|EMBL:ABL04956.1}; GN OrderedLocusNames=MUL_2628 {ECO:0000313|EMBL:ABL04956.1}; OS Mycobacterium ulcerans (strain Agy99). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL04956.1, ECO:0000313|Proteomes:UP000000765}; RN [1] {ECO:0000313|EMBL:ABL04956.1, ECO:0000313|Proteomes:UP000000765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL04956.1, RC ECO:0000313|Proteomes:UP000000765}; RX PubMed=17210928; DOI=10.1101/gr.5942807; RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F., RA Laval F., Daffe M., Parkhill J., Cole S.T.; RT "Reductive evolution and niche adaptation inferred from the genome of RT Mycobacterium ulcerans, the causative agent of Buruli ulcer."; RL Genome Res. 17:192-200(2007). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole CC ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR). {ECO:0000256|HAMAP-Rule:MF_01928}. CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole CC ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR). {ECO:0000256|RuleBase:RU361200}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CC hydrogencarbonate + ATP = 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole + ADP + phosphate + 2 H(+); Xref=Rhea:RHEA:19317, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:456216; EC=6.3.4.18; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; 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:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928, CC ECO:0000256|RuleBase:RU361200}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP- CC Rule:MF_01928, ECO:0000256|RuleBase:RU361200}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000325; ABL04956.1; -; Genomic_DNA. DR AlphaFoldDB; A0PRI7; -. DR KEGG; mul:MUL_2628; -. DR eggNOG; COG0026; Bacteria. DR HOGENOM; CLU_011534_0_2_11; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000765; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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 FunFam; 3.30.470.20:FF:000029; N5-carboxyaminoimidazole ribonucleotide synthase; 1. DR FunFam; 3.40.50.20:FF:000025; N5-carboxyaminoimidazole ribonucleotide synthase; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; IPR054350; PurT/PurK_preATP-grasp. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; NF004679; PRK06019.1-5; 1. DR NCBIfam; NF004680; PRK06019.1-6; 1. DR NCBIfam; TIGR01161; purK; 1. DR PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1. DR PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1. DR Pfam; PF02222; ATP-grasp; 1. DR Pfam; PF17769; PurK_C; 1. DR Pfam; PF22660; RS_preATP-grasp-like; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01928}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01928}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01928}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01928}; Reference proteome {ECO:0000313|Proteomes:UP000000765}. FT DOMAIN 133..325 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 209..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 295..296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" SQ SEQUENCE 424 AA; 45425 MW; C8D9415CD8473C34 CRC64; MIHNDLVLQP PNTPVMGHDT MMAVPSSRTP QVAMVGGGQL ARMTHQAAIA LGQNLRVLVN SADDPAAQVT PNVVIGSHTD LDDLRRIAAG ADVVTFDHEH VPAELLDKLV AEGVVLAPPP QALVHAQDKL VMRRRLQALD VPVPRYLGIH QLEELGELDA FARQLDAPLV VKAVRGGYDG RGVQMARDLA DARDIASGYL AGGVPVLVEE RVQLRRELSA LVARSPFGQG AAWPVVETVQ QDGICVAVIA PAPALSAQAG ADAQQLALRL AAELGVVGVL AVELFETTDG ALVVNELAMR PHNSGHWTMD GSRTSQFEQH LRAVLDYPLG DTEAIAPVTV MTNVLGAAAQ PAMSLDERLH HLFARMPDAR VHLYGKDERP GRKVGHINFL GFDPAAVAGL RERAELAAHW LSHGQWTDGW DPHG //