ID F9URK4_LACPL Unreviewed; 376 AA. AC F9URK4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 18-JAN-2017, entry version 44. 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 OrderedLocusNames=lp_2728 {ECO:0000313|EMBL:CCC79843.1}; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. 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., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA 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. CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000256|HAMAP-Rule:MF_01928}. CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000256|RuleBase:RU361200}. 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. {ECO:0000256|HAMAP-Rule:MF_01928, CC ECO:0000256|RuleBase:RU361200}. 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 {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 ECO:0000256|SAAS:SAAS00653163}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP- CC Rule:MF_01928}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 ProteinModelPortal; F9URK4; -. DR STRING; 220668.lp_2728; -. DR EnsemblBacteria; CCC79843; CCC79843; lp_2728. DR GeneID; 1063026; -. DR KEGG; lpl:lp_2728; -. DR eggNOG; ENOG4105CY8; Bacteria. DR eggNOG; COG0026; LUCA. DR KO; K01589; -. DR OMA; DSPCGQV; -. DR BioCyc; LPLA220668:G137Z-2324-MONOMER; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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-HAMAP. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 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; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR005875; PurK. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR Pfam; PF02222; ATP-grasp; 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|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00653136}; KW Complete proteome {ECO:0000313|Proteomes:UP000000432}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200}; Lyase {ECO:0000313|EMBL:CCC79843.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00653153}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00653155}; KW Reference proteome {ECO:0000313|Proteomes:UP000000432}. FT DOMAIN 115 300 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT NP_BIND 156 162 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT NP_BIND 270 271 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 111 111 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 151 151 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 193 193 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 216 216 ATP. {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 //