ID A0A1B7W1C0_APHFL Unreviewed; 533 AA. AC A0A1B7W1C0; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 29-MAY-2024, entry version 39. DE RecName: Full=Bifunctional pantoate ligase/cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_01349}; DE Includes: DE RecName: Full=Pantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_01349}; DE Short=PS {ECO:0000256|HAMAP-Rule:MF_01349}; DE EC=6.3.2.1 {ECO:0000256|HAMAP-Rule:MF_01349}; DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_01349}; DE AltName: Full=Pantoate-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01349}; DE Includes: DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_01349}; DE Short=CK {ECO:0000256|HAMAP-Rule:MF_01349}; DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_01349}; DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01349}; DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_01349}; GN Name=panC/cmk {ECO:0000256|HAMAP-Rule:MF_01349}; GN ORFNames=AN481_02255 {ECO:0000313|EMBL:OBQ27086.1}; OS Aphanizomenon flos-aquae LD13. OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae; OC Aphanizomenon. OX NCBI_TaxID=1710894 {ECO:0000313|EMBL:OBQ27086.1, ECO:0000313|Proteomes:UP000092382}; RN [1] {ECO:0000313|EMBL:OBQ27086.1, ECO:0000313|Proteomes:UP000092382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDT13 {ECO:0000313|EMBL:OBQ27086.1}; RA Driscoll C.; RT "Whole genome shotgun sequence assembly of Aphanizomenon flos-aquae RT UKL13."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in CC an ATP-dependent reaction via a pantoyl-adenylate intermediate. CC {ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- FUNCTION: Catalyzes the transfer of a phosphate group from ATP to CC either CMP or dCMP to form CDP or dCDP and ADP, respectively. CC {ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + CC diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; CC Evidence={ECO:0000256|ARBA:ARBA00001155, ECO:0000256|HAMAP- CC Rule:MF_01349}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.25; CC Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|HAMAP- CC Rule:MF_01349}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.25; CC Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP- CC Rule:MF_01349}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)- CC pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC {ECO:0000256|ARBA:ARBA00004990, ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily. CC {ECO:0000256|ARBA:ARBA00009427}. CC -!- SIMILARITY: Belongs to the pantothenate synthetase family. CC {ECO:0000256|ARBA:ARBA00009256}. CC -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase CC family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- SIMILARITY: In the N-terminal section; belongs to the pantothenate CC synthetase family. {ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OBQ27086.1}. 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; LJOY01000004; OBQ27086.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1B7W1C0; -. DR STRING; 1803587.GCA_001593825_02919; -. DR PATRIC; fig|1710894.3.peg.380; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000092382; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IEA:TreeGrafter. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd02020; CMPK; 1. DR CDD; cd00560; PanC; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 1. DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1. DR HAMAP; MF_00158; PanC; 1. DR HAMAP; MF_01349; PanCY; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR003136; Cytidylate_kin. DR InterPro; IPR011994; Cytidylate_kinase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003721; Pantoate_ligase. DR InterPro; IPR024894; Pantoate_ligase/cytidylate_kin. DR InterPro; IPR042176; Pantoate_ligase_C. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00017; cmk; 1. DR NCBIfam; TIGR00125; cyt_tran_rel; 1. DR NCBIfam; TIGR00018; panC; 1. DR PANTHER; PTHR21299:SF2; CYTIDYLATE KINASE; 1. DR PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1. DR Pfam; PF02224; Cytidylate_kin; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01349}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01349}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01349}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01349, ECO:0000313|EMBL:OBQ27086.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01349}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01349}; KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655, KW ECO:0000256|HAMAP-Rule:MF_01349}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01349}. FT DOMAIN 312..529 FT /note="Cytidylate kinase" FT /evidence="ECO:0000259|Pfam:PF02224" FT REGION 1..299 FT /note="Pantoate--beta-alanine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT REGION 300..533 FT /note="Cytidylate kinase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT ACT_SITE 52 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 45..52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 76 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 76 FT /ligand="beta-alanine" FT /ligand_id="ChEBI:CHEBI:57966" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 169..172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 175 FT /ligand="(R)-pantoate" FT /ligand_id="ChEBI:CHEBI:15980" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" FT BINDING 206..209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01349" SQ SEQUENCE 533 AA; 59050 MW; BA9AAB067D8566B7 CRC64; MRVLTNVVAL RCYLNRRRWQ SHLKPPDDDE QTSWYPTVVG LVPTMGNLHQ GHLSLIKRAR RENSTVIVSI FVNPLQFGPN EDYQRYPRTL EQDRQFCEQA GVDVIFAPTP EEIGIPSKNI AETRMTQVVP PSDMMSGLCG NCRPGHFAGV ATIVTKLLNL VQPDRAYFGQ KDGQQLAIIK RLVADLNLPV EIVVCPTVRE VSGLALSSRN QYLTATEKEQ ATVLFKGLRQ AEAAFKAGVR HSSKLIALVR EEIAKVRAIS LEYVELVEPT TLMFLEKVEN EGMLAIAARL GSTRLIDNTI LRDKDQIREP IIAIDGPAGA GKSTVARQVA QELGLVYLDT GAMYRAIAWL VLEQGIAIDD DCAVAELATR CKIELTPGQS LQSPVKVQIN DIDVTEKIRT VEVTSLVSVI AAQSAVRQAL VQQQQSWGQR GGLVAEGRDI GTHVFPDAEV KIFLTASVGE RARRRHQDFQ ARNQNQVSLE QLERDIAERD LKDSTRKISP LQKAADAIEV ETDGLTASEV AAQIINHYQR LSD //