ID A0A1E7Q1U0_9GAMM Unreviewed; 231 AA. AC A0A1E7Q1U0; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 15-MAR-2017, entry version 3. 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; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=1628148 {ECO:0000313|EMBL:OEY68165.1}; RN [1] {ECO:0000313|EMBL:OEY68165.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KH87 {ECO:0000313|EMBL:OEY68165.1}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; 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 ECO:0000256|SAAS:SAAS00384421}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00384435}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|SAAS:SAAS00611758}; 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 -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00384485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00701620}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274, CC ECO:0000256|SAAS:SAAS00384519}. CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00701623}. 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: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 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 PANTHER; PTHR34265; PTHR34265; 1. 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 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, ECO:0000313|EMBL:OEY68165.1}; 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:SAAS00461364}; 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 89 92 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01274}. FT ACT_SITE 91 91 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01274}. FT METAL 112 112 Monovalent cation. {ECO:0000256|HAMAP- FT Rule:MF_01274}. FT BINDING 82 82 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01274}. FT BINDING 115 115 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}. FT BINDING 167 167 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //