ID F9URK4_LACPL Unreviewed; 376 AA. AC F9URK4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 12-OCT-2022, entry version 72. 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=purK1 {ECO:0000313|EMBL:CCC79843.1}; GN Synonyms=purK {ECO:0000256|HAMAP-Rule:MF_01928, GN ECO:0000256|RuleBase:RU361200}; GN ORFNames=lp_2728 {ECO:0000313|EMBL:CCC79843.1}; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC79843.1, ECO:0000313|Proteomes:UP000000432}; RN [1] {ECO:0000313|EMBL:CCC79843.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W., RA Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R., RA de Vries M., Ursing B., de Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WCFS1; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CCC79843.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=22156394; DOI=10.1128/JB.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). 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 + 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:0000256|HAMAP-Rule:MF_01928, CC 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; AL935263; CCC79843.1; -; Genomic_DNA. DR RefSeq; WP_011101896.1; NC_004567.2. DR RefSeq; YP_004890357.1; NC_004567.2. DR STRING; 220668.lp_2728; -. DR EnsemblBacteria; CCC79843; CCC79843; lp_2728. DR GeneID; 57026103; -. DR KEGG; lpl:lp_2728; -. DR PATRIC; fig|220668.9.peg.2283; -. DR eggNOG; COG0026; Bacteria. DR HOGENOM; CLU_011534_0_1_9; -. DR OMA; ITFDHEH; -. DR PhylomeDB; F9URK4; -. DR BioCyc; LPLA220668:G1GW0-2334-MON; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000432; Chromosome. 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:UniProtKB-KW. DR GO; GO:0051287; F:NAD 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; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR005875; PurK. DR InterPro; IPR040686; PurK_C. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02826; 2-Hacid_dh_C; 1. 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01928}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; KW Lyase {ECO:0000313|EMBL:CCC79843.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01928}; Reference proteome {ECO:0000313|Proteomes:UP000000432}. FT DOMAIN 115..300 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 111 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 151 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 156..162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 216 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 270..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" SQ SEQUENCE 376 AA; 40503 MW; FC3B974763F63621 CRC64; MNANFKEALL PPATIGIVGG GQLGQMMTLS AKAMGYRVGV LDPTPKAPAA QVADFQIVAA YDDQAALLDL ARRSDVLTYE FENVDENALI AAQAYAKLPQ GTALLHITGD RLNEKQFLHD HGIPVTSFAP VTDLQSLNYA LNRVGTPAIL KTAAGGYDGH GQTDLDTAVV TKAASALLTQ PCILEARQKF RTEVSMMVTR SAAGVVTTFP LVENQHQHHI LHTTIAPANV QPSVHSAARK IAVSIAESLE LRGVLGIEFF VLPDDTLLVN ELAPRPHNSG HYTIEACNIS QFEAHIRSIC GLPIPAITQT SPAVMRNLLG DDLTVARQQL VEHPEWHFHD YGKAAIKPQR KMGHVTVLNH DIDAALASLA NLKGEQ //