ID Q47IX3_DECAR Unreviewed; 386 AA. AC Q47IX3; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 116. 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}; GN OrderedLocusNames=Daro_0451 {ECO:0000313|EMBL:AAZ45208.1}; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae; OC Dechloromonas. OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ45208.1}; RN [1] {ECO:0000313|EMBL:AAZ45208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RCB {ECO:0000313|EMBL:AAZ45208.1}; RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.; RT "Complete sequence of Dechloromonas aromatica RCB."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; CP000089; AAZ45208.1; -; Genomic_DNA. DR AlphaFoldDB; Q47IX3; -. DR STRING; 159087.Daro_0451; -. DR KEGG; dar:Daro_0451; -. DR eggNOG; COG0026; Bacteria. DR HOGENOM; CLU_011534_0_1_4; -. DR UniPathway; UPA00074; UER00942. 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 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; IPR011054; Rudment_hybrid_motif. 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 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|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; KW Lyase {ECO:0000313|EMBL:AAZ45208.1}; 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}. FT DOMAIN 114..298 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 149 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 154..160 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 184..187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 192 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 268..269 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" SQ SEQUENCE 386 AA; 42057 MW; 31964C1849260870 CRC64; MPVKSAMILP PATLGMLGGG QLGRFFVSAA HELGYQVWVL DPDKNSPAGQ IAERHFCVDY NDYAALDEFA AGCAAITTEF ENVPADTLDY LAKFVPVRPS AAAVGICQNR IAEKSFLRDN GLPHGPFAAI RCEDDIRNAD ASLFPAILKV ARFGYDGKGQ ATVHNREEAL VAFGQFKGEQ CVLEQRLTLD YEVSVVLARD ERGRVACFPT GENQHTKGIL DVSIVPARTT ACVKSDAEEV AARIAEKLGY IGTMGVEFFI SRGQLIVNEM APRPHNSGHY TIDACVTDQF EQQVRALCGL PLGEPRAHSA SVMVNLLGDL WYDGETYREP DWAKLHAVPN LKLHLYGKHH ARPGRKMGHF TVIGDNAEAV QKAALAARAA IGIRDE //