ID COAE_HAEIN Reviewed; 206 AA. AC P44920; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 04-NOV-2026, entry version 156. DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376}; DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376}; DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376}; GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; GN OrderedLocusNames=HI_0890; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of CC dephosphocoenzyme A to form coenzyme A. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00376}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}. CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP- CC Rule:MF_00376, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22550.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; L42023; AAC22550.1; ALT_INIT; Genomic_DNA. DR PIR; A64161; A64161. DR PDB; 1JJV; X-ray; 2.00 A; A=1-206. DR AlphaFoldDB; P44920; -. DR SMR; P44920; -. DR STRING; 71421.HI_0890; -. DR EnsemblBacteria; AAC22550; AAC22550; HI_0890. DR KEGG; hin:HI_0890; -. DR PATRIC; fig|71421.8.peg.932; -. DR eggNOG; COG0237; Bacteria. DR HOGENOM; CLU_057180_1_2_6; -. DR OMA; AAAHWII; -. DR OrthoDB; 9812943at2; -. DR PhylomeDB; P44920; -. DR BioCyc; HINF71421:G1GJ1-930-MONOMER; -. DR BRENDA; 2.7.1.24; 2529. DR UniPathway; UPA00241; UER00356. DR EvolutionaryTrace; P44920; -. DR Proteomes; UP000000579; Chromosome. 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; IBA:GO_Central. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central. DR CDD; cd02022; DPCK; 1. DR FunFam; 3.40.50.300:FF:000518; Dephospho-CoA kinase; 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 NCBIfam; TIGR00152; dephospho-CoA kinase; 1. 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 PROSITE; PS51219; DPCK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..206 FT /note="Dephospho-CoA kinase" FT /id="PRO_0000172947" FT DOMAIN 4..204 FT /note="DPCK" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376" FT BINDING 12..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:1JJV" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:1JJV" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 32..38 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 45..54 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 67..75 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 78..101 FT /evidence="ECO:0007829|PDB:1JJV" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:1JJV" FT TURN 113..119 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:1JJV" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 134..141 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 149..158 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 162..168 FT /evidence="ECO:0007829|PDB:1JJV" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:1JJV" FT HELIX 179..203 FT /evidence="ECO:0007829|PDB:1JJV" SQ SEQUENCE 206 AA; 23287 MW; DF85B65D50131C01 CRC64; MTYIVGLTGG IGSGKTTIAN LFTDLGVPLV DADVVAREVV AKDSPLLSKI VEHFGAQILT EQGELNRAAL RERVFNHDED KLWLNNLLHP AIRERMKQKL AEQTAPYTLF VVPLLIENKL TALCDRILVV DVSPQTQLAR SAQRDNNNFE QIQRIMNSQV SQQERLKWAD DVINNDAELA QNLPHLQQKV LELHQFYLQQ AENKNA //