ID A0A1E7Q1U0_9GAMM Unreviewed; 231 AA. AC A0A1E7Q1U0; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 07-OCT-2020, entry version 14. 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=BI198_00250 {ECO:0000313|EMBL:OEY68165.1}; OS Rheinheimera salexigens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Rheinheimera. OX NCBI_TaxID=1628148 {ECO:0000313|EMBL:OEY68165.1, ECO:0000313|Proteomes:UP000242258}; RN [1] {ECO:0000313|Proteomes:UP000242258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH87 {ECO:0000313|Proteomes:UP000242258}; RA Wan X., Hou S.; RL Submitted (SEP-2016) 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:OEY68165.1}. 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; MKEK01000001; OEY68165.1; -; Genomic_DNA. DR RefSeq; WP_070047732.1; NZ_MKEK01000001.1. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000242258; 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 HAMAP; MF_01274; Pantothen_kinase_3; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR004619; Type_III_PanK. DR PANTHER; PTHR34265; PTHR34265; 1. DR Pfam; PF03309; Pan_kinase; 1. DR SUPFAM; SSF53067; SSF53067; 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:OEY68165.1}; 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:UP000242258}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01274}. FT NP_BIND 6..13 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT REGION 89..92 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT ACT_SITE 91 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT METAL 112 FT /note="Monovalent cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 82 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 115 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" FT BINDING 167 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274" SQ SEQUENCE 231 AA; 25065 MW; 72D74A7F91CC55F5 CRC64; MYLLLDIGNT RCKAALYENG SLRLVQDLAT MDINPTDIEA VIVASVAADE QLQVLKQKLK LTDVRWIQVQ SEAAAFGIRN SYSEPEKLGV DRWLAMIAAK QQLPNHSIMV IDAGTAVTID WLDPQGSHQG GWIIPGLAMQ QRAVVSNTAK VLNANEFKPV LAPANNTATA LQSGCLAAVI GAIQLAWQNH PTQQIILTGG DSLLLASHLD SLPIIIEPLL VFHGLSRYCR L //