ID K0JR33_SACES Unreviewed; 261 AA. AC K0JR33; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 28-JUN-2023, entry version 54. DE RecName: Full=Type III pantothenate kinase {ECO:0000256|HAMAP-Rule:MF_01274}; DE EC=2.7.1.33 {ECO:0000256|HAMAP-Rule:MF_01274}; DE AltName: Full=PanK-III {ECO:0000256|HAMAP-Rule:MF_01274}; DE AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_01274}; GN Name=coaX {ECO:0000256|HAMAP-Rule:MF_01274, GN ECO:0000313|EMBL:CCH27697.1}; GN OrderedLocusNames=BN6_03660 {ECO:0000313|EMBL:CCH27697.1}; OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC OS 15066 / NRRL 15764). OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharothrix. OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH27697.1, ECO:0000313|Proteomes:UP000006281}; RN [1] {ECO:0000313|EMBL:CCH27697.1, ECO:0000313|Proteomes:UP000006281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764 RC {ECO:0000313|Proteomes:UP000006281}; RX PubMed=22958348; DOI=10.1186/1471-2164-13-465; RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J., RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.; RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and RT comparison to the other completely sequenced Pseudonocardiaceae."; RL BMC Genomics 13:465-465(2012). CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the CC first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + CC H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; CC EC=2.7.1.33; Evidence={ECO:0000256|ARBA:ARBA00001206, CC ECO:0000256|HAMAP-Rule:MF_01274}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|ARBA:ARBA00001958}; CC -!- COFACTOR: CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01274}; CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01274}; CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000256|HAMAP- CC Rule:MF_01274}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 1/5. {ECO:0000256|ARBA:ARBA00005225, CC ECO:0000256|HAMAP-Rule:MF_01274}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274}. CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_01274}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}. 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; HE804045; CCH27697.1; -; Genomic_DNA. DR RefSeq; WP_015097811.1; NC_019673.1. DR AlphaFoldDB; K0JR33; -. DR STRING; 1179773.BN6_03660; -. DR EnsemblBacteria; CCH27697; CCH27697; BN6_03660. DR KEGG; sesp:BN6_03660; -. DR PATRIC; fig|1179773.3.peg.373; -. DR eggNOG; COG1521; Bacteria. DR HOGENOM; CLU_066627_1_0_11; -. DR OMA; HEPWLTL; -. DR OrthoDB; 9804707at2; -. DR BioCyc; SESP1179773:BN6_RS01795-MON; -. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000006281; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_01274; Pantothen_kinase_3; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR004619; Type_III_PanK. DR PANTHER; PTHR34265; TYPE III PANTOTHENATE KINASE; 1. DR PANTHER; PTHR34265:SF1; TYPE III PANTOTHENATE KINASE; 1. DR Pfam; PF03309; Pan_kinase; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR TIGRFAMs; TIGR00671; baf; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274}; KW Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP- KW Rule:MF_01274}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01274}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000313|EMBL:CCH27697.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01274}; KW Reference proteome {ECO:0000313|Proteomes:UP000006281}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000313|EMBL:CCH27697.1}. FT ACT_SITE 111 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 6..13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 109..112 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 131 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" SQ SEQUENCE 261 AA; 27793 MW; A31EB370C92CEE4E CRC64; MLLAIDVGNT NIVLGLYDGT GDKAALVRDW RMRTDARMTA DELALTMRGL LGEYADKITG ISALSTVPAV LRELRVMLGR YYSAVPKVLV EPGVRTGVPL LVDNPKEVGS DRVINTLAAH HLHSTACVVV DFGTSTNLDV ISAKGEFLGG ALAPGIEISV DALAARAAQL RKVELVRPRS VIGKNTVECL QSGIVYGFVG QVDGLVRRIV DELQVSEPGP VTVIATGGLA PLVVTESATI HAHVPDLTLL GLRLVFERNM R //