ID A0A231VUQ4_9MICC Unreviewed; 205 AA. AC A0A231VUQ4; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 22-FEB-2023, entry version 17. DE RecName: Full=Dephospho-CoA kinase {ECO:0000256|HAMAP-Rule:MF_00376}; DE EC=2.7.1.24 {ECO:0000256|HAMAP-Rule:MF_00376}; DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000256|HAMAP-Rule:MF_00376}; GN Name=coaE {ECO:0000256|HAMAP-Rule:MF_00376}; GN ORFNames=B9K03_05390 {ECO:0000313|EMBL:OXT11814.1}; OS Rothia sp. Olga. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia. OX NCBI_TaxID=1979525 {ECO:0000313|EMBL:OXT11814.1, ECO:0000313|Proteomes:UP000215251}; RN [1] {ECO:0000313|EMBL:OXT11814.1, ECO:0000313|Proteomes:UP000215251} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Olga {ECO:0000313|EMBL:OXT11814.1, RC ECO:0000313|Proteomes:UP000215251}; RA Kim Y., Blasche S., Patil K.R.; RT "Kefir bacterial isolates."; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of CC dephosphocoenzyme A to form coenzyme A. {ECO:0000256|HAMAP- CC Rule:MF_00376}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; CC EC=2.7.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00376}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00376}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376}. CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000256|HAMAP- CC Rule:MF_00376}. 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:OXT11814.1}. 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; NDFM01000003; OXT11814.1; -; Genomic_DNA. DR AlphaFoldDB; A0A231VUQ4; -. DR EnsemblBacteria; OXT11814; OXT11814; B9K03_05390. DR UniPathway; UPA00241; UER00356. DR Proteomes; UP000215251; 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:0004140; F:dephospho-CoA 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 CDD; cd02022; DPCK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1. DR InterPro; IPR001977; Depp_CoAkinase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10695:SF46; BIFUNCTIONAL COENZYME A SYNTHASE-RELATED; 1. DR PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1. DR Pfam; PF01121; CoaE; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00152; dephospho-CoA kinase; 1. DR PROSITE; PS51219; DPCK; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00376}; KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:OXT11814.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00376}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376}. FT BINDING 16..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376" SQ SEQUENCE 205 AA; 22286 MW; 826B2BAE716B92A1 CRC64; MTEKTLRRYA ITGGIGSGKS TVAAMFARLG AVIIDADAIS RDLMRPTENT LNAVVAEFGP DILHPDGTLN RPALAALVFS NEDARTRLNN IVHPAVRARA DALVEQAWRA PGFSGIIIDD IPLLAETNRA AEFDGVIVVR TSLEKRLTRL TKTRGMAEED ARARIAAQAT DTQRAAIATW IIDNDGSAEN TQTQVERIWA LMTNH //