ID A0A263NW34_9PSED Unreviewed; 249 AA. AC A0A263NW34; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 03-MAY-2023, entry version 21. 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 ORFNames=B7453_10725 {ECO:0000313|EMBL:OZO04599.1}; OS Pseudomonas sp. IB20. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1702250 {ECO:0000313|EMBL:OZO04599.1, ECO:0000313|Proteomes:UP000215734}; RN [1] {ECO:0000313|EMBL:OZO04599.1, ECO:0000313|Proteomes:UP000215734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IB20 {ECO:0000313|EMBL:OZO04599.1, RC ECO:0000313|Proteomes:UP000215734}; RA Lira F., Olivares Pacheco J.A.; RT "Antartic Pseudomonas sp. IB20 genome sequencing and assembly."; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. 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: 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:OZO04599.1}. 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; NMRE01000019; OZO04599.1; -; Genomic_DNA. DR AlphaFoldDB; A0A263NW34; -. DR EnsemblBacteria; OZO04599; OZO04599; B7453_10725. DR OrthoDB; 9781305at2; -. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000215734; 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: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:OZO04599.1}; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_01274}. FT ACT_SITE 102 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 93 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 100..103 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 122 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 125 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 181 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" SQ SEQUENCE 249 AA; 26768 MW; 41B1B67A684A998A CRC64; MILELDCGNS FIKWRVLGSA IASASAEGIV GSDLALIESL IAIPGLLLTR CRLVSVRASE ETGKLVEALQ EAFGVTVSCA APAREMAGVR NGYEEFERLG LDRWLAMLGG FKLASGNCLV LDFGTAATAD FIATDGEHLG GFICPGMPLM RSQLRTHTRK IRYDDAAAEQ AMERLSPGRT TVEAVERGCT LMLRGFVLTQ LELARRYWGD DFTVFLTGGD ADLVSDAVPQ ARFVPDLVFV GLAMACPLS //