ID   COAE_MYCPN              Reviewed;         200 AA.
AC   P75400;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-JUN-2026, entry version 127.
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=MPN_382; ORFNames=MP455;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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}.
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DR   EMBL; U00089; AAB96103.1; -; Genomic_DNA.
DR   PIR; S73781; S73781.
DR   RefSeq; WP_010874738.1; NC_000912.1.
DR   AlphaFoldDB; P75400; -.
DR   SMR; P75400; -.
DR   STRING; 272634.MPN_382; -.
DR   PaxDb; 272634-MPN_382; -.
DR   EnsemblBacteria; AAB96103; AAB96103; MPN_382.
DR   GeneID; 66608960; -.
DR   KEGG; mpn:MPN_382; -.
DR   HOGENOM; CLU_057180_4_0_14; -.
DR   OrthoDB; 399073at2; -.
DR   BioCyc; MPNE272634:G1GJ3-605-MONOMER; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000000808; 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   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   NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..200
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000172962"
FT   DOMAIN          2..200
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   200 AA;  22910 MW;  396EA0C4AA940589 CRC64;
     MLIAVVGKAG VGKTTVLQYI ADYFHFPVFF ADRFIHQQYA NGQAGYAIVK QQFGAQFVNH
     EAVDRKQLAQ YVFNQPDELK RLSNLTKPLV QEWLNQLKAQ FQDKIALVEI AVMLNYWNDY
     RPFFDEVIQI ERDAKIVKQA LKARGVDVEQ VQKLIADPTY PILTVINNST VAECALHVTQ
     FLESIAKSDK CHHGHYQTPK
//