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COAE_STRPN
ID   COAE_STRPN              Reviewed;         201 AA.
AC   Q97R60;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=SP_0971;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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}.
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DR   EMBL; AE005672; AAK75092.1; -; Genomic_DNA.
DR   PIR; C95112; C95112.
DR   RefSeq; WP_000516207.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97R60; -.
DR   SMR; Q97R60; -.
DR   STRING; 170187.SP_0971; -.
DR   EnsemblBacteria; AAK75092; AAK75092; SP_0971.
DR   KEGG; spn:SP_0971; -.
DR   eggNOG; COG0237; Bacteria.
DR   OMA; QMDIEQK; -.
DR   PhylomeDB; Q97R60; -.
DR   BioCyc; SPNE170187:G1FZB-999-MON; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000000585; 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; 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; 3.40.50.300; -; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00152; TIGR00152; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..201
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000173012"
FT   DOMAIN          4..201
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"
SQ   SEQUENCE   201 AA;  23005 MW;  A7430A1D1FABF814 CRC64;
     MGKIIGITGG IASGKSTVTN FLRQQGFQVV DADAVVHQLQ KPGGRLFEAL VQHFGQEIIL
     ENGELNRPLL ASLIFSNPDE REWSKQIQGE IIREELATLR EQLAQTEEIF FMDIPLLFEQ
     DYSDWFAETW LVYVDRDAQV ERLMKRDQLS KDEAESRLAA QWPLEKKKDL ASQVLDNNGN
     QNQLLNQVHI LLEGGRQDDR D
 
 
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