ID A4XJY4_CALS8 Unreviewed; 384 AA. AC A4XJY4; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Csac_1629 {ECO:0000313|EMBL:ABP67219.1}; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T OS 6331). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP67219.1, ECO:0000313|Proteomes:UP000000256}; RN [1] {ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331 RC {ECO:0000313|Proteomes:UP000000256}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., RA Kengen S.M.W., Richardson P.; RT "Genome sequence of the thermophilic hydrogen-producing bacterium RT Caldicellulosiruptor saccharolyticus DSM 8903."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABP67219.1, ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331 RC {ECO:0000313|Proteomes:UP000000256}; RX PubMed=18776029; DOI=10.1128/AEM.00968-08; RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K., RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E., RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J., RA Kelly R.M., Kengen S.W.; RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor RT saccharolyticus."; RL Appl. Environ. Microbiol. 74:6720-6729(2008). 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; CP000679; ABP67219.1; -; Genomic_DNA. DR RefSeq; WP_011917154.1; NC_009437.1. DR AlphaFoldDB; A4XJY4; -. DR STRING; 351627.Csac_1629; -. DR KEGG; csc:Csac_1629; -. DR eggNOG; COG0026; Bacteria. DR HOGENOM; CLU_011534_0_2_9; -. DR OrthoDB; 9804625at2; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000256; 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: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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01928}; 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..296 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 148 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 179..182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" FT BINDING 266..267 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928" SQ SEQUENCE 384 AA; 42589 MW; CC1F140EE4EECC9F CRC64; MNKGVFGYPL MKIGIIGGGQ LGKMLSQKAK QMGFYVISLD PSAACPAASV SDELIVSDFY SPEKLKELVE KSDITTYEIE HINTSVLKEL YDEGYNILPS PYCLEIIQDK LKQKQVLQSA GLPVPRFERV ESFDISFFEN FGFPLVQKAT KGGYDGRGVV VLKSKDDINK VLKTESYIEE FVDVEKELAV IVARNKKGDV VSYPVVEMVF DETANILDIL IVPARVEKDI EDEAKKIAIK AVEALQGVGV FGVELFLTKD RKILINEIAP RPHNSGHYTI EACITSQFEQ HLRAICDLPL GSTKLLSPAV MINLLGDDGY KGTPVIEGLI DALSIEGVSF HFYGKKVTAP FRKMGHVTIL DDNLERAIEK AKKVKEVLKI KSEV //