ID K0JR33_SACES Unreviewed; 261 AA. AC K0JR33; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 29-APR-2015, entry version 19. 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 / OS NBRC 15066 / NRRL 15764). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; 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 ECO:0000256|SAAS:SAAS00088441}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00088447}. CC -!- COFACTOR: CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01274}; CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01274}; CC Note=A monovalent cation. Ammonium or potassium. CC {ECO:0000256|HAMAP-Rule:MF_01274}; CC -!- COFACTOR: CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; CC Evidence={ECO:0000256|SAAS:SAAS00173384}; CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|SAAS:SAAS00173384}; CC Note=A monovalent cation. Ammonium or potassium. CC {ECO:0000256|SAAS:SAAS00173384}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00088429}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00088433}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00088436}. CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family. CC {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 RefSeq; YP_007034570.1; NC_019673.1. DR EnsemblBacteria; CCH27697; CCH27697; BN6_03660. DR KEGG; sesp:BN6_03660; -. DR KO; K03525; -. DR OMA; LENHYAR; -. 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-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01274; Pantothen_kinase_3; 1. DR InterPro; IPR004619; Type_III_PanK. DR Pfam; PF03309; Pan_kinase; 1. DR TIGRFAMs; TIGR00671; baf; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00088442}; KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00088444}; KW Complete proteome {ECO:0000313|Proteomes:UP000006281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00088451}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00088438}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00088446}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00173372}; KW Reference proteome {ECO:0000313|Proteomes:UP000006281}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01274, KW ECO:0000256|SAAS:SAAS00088435}. FT NP_BIND 6 13 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}. FT REGION 109 112 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01274}. FT ACT_SITE 111 111 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01274}. FT METAL 131 131 Monovalent cation. {ECO:0000256|HAMAP- FT Rule:MF_01274}. FT BINDING 134 134 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //