ID A0A1B7W1C0_APHFL Unreviewed; 533 AA. AC A0A1B7W1C0; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 08-MAY-2019, entry version 21. 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-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01349}; DE AltName: Full=Pantoate--beta-alanine ligase {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; Cyanobacteria; 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 CC in 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 + CC AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, CC ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01349, ECO:0000256|SAAS:SAAS01125062}; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01349, ECO:0000256|SAAS:SAAS01150952}; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01349, ECO:0000256|SAAS:SAAS01150969}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01349, ECO:0000256|SAAS:SAAS00094317}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01349}. CC -!- SIMILARITY: In the C-terminal section; belongs to the cytidylate CC kinase family. Type 1 subfamily. {ECO:0000256|HAMAP- CC 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; OBQ27086; OBQ27086; AN481_02255. DR PATRIC; fig|1710894.3.peg.380; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000092382; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. 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; -; 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; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02224; Cytidylate_kin; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00017; cmk; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00018; panC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01349, KW ECO:0000256|SAAS:SAAS00464754}; KW Complete proteome {ECO:0000313|Proteomes:UP000092382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01349}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01349, KW ECO:0000256|SAAS:SAAS01150975, ECO:0000313|EMBL:OBQ27086.1}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01349, KW ECO:0000256|SAAS:SAAS00464803, ECO:0000313|EMBL:OBQ27086.1}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01349}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01349, KW ECO:0000256|SAAS:SAAS00464749}; KW Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_01349, KW ECO:0000256|SAAS:SAAS00464740}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01349, KW ECO:0000256|SAAS:SAAS01150965, ECO:0000313|EMBL:OBQ27086.1}. FT DOMAIN 312 529 Cytidylate_kin. {ECO:0000259|Pfam: FT PF02224}. FT NP_BIND 45 52 ATP. {ECO:0000256|HAMAP-Rule:MF_01349}. FT NP_BIND 169 172 ATP. {ECO:0000256|HAMAP-Rule:MF_01349}. FT NP_BIND 206 209 ATP. {ECO:0000256|HAMAP-Rule:MF_01349}. FT REGION 1 299 Pantoate--beta-alanine ligase. FT {ECO:0000256|HAMAP-Rule:MF_01349}. FT REGION 300 533 Cytidylate kinase. {ECO:0000256|HAMAP- FT Rule:MF_01349}. FT ACT_SITE 52 52 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01349}. FT BINDING 76 76 Beta-alanine. {ECO:0000256|HAMAP-Rule: FT MF_01349}. FT BINDING 76 76 Pantoate. {ECO:0000256|HAMAP-Rule: FT MF_01349}. FT BINDING 175 175 Pantoate. {ECO:0000256|HAMAP-Rule: FT MF_01349}. FT BINDING 198 198 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT 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 //