ID   COAE_CORGT              Reviewed;         195 AA.
AC   P56187;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
DE   Flags: Fragment;
GN   Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376};
OS   Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OG   Plasmid pBSBG2.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13869 / DSM 1412 / NCIMB 9567 / 2256;
RA   Yoon K.-H.;
RT   "Cloning and nucleotide sequence of enzyme II of Brevibacterium
RT   lactofermentum phosphotransferase system.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Rudd K.E.;
RL   Unpublished observations (JAN-1997).
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; L18875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P56187; -.
DR   SMR; P56187; -.
DR   UniPathway; UPA00241; UER00356.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
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; Plasmid; Transferase.
FT   CHAIN           1..>195
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000172937"
FT   DOMAIN          3..>195
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   NON_TER         195
SQ   SEQUENCE   195 AA;  21135 MW;  D7F0333860E0BDD3 CRC64;
     MLKIGLTGGI GSGKSTVADL LSSEGFLIID ADQIAREIVE PGQPALAELV EAFGPEIIKE
     DGSLDRQGLA AKAFVDAEHT ALLNSITHPR IAEETARRFA EAEANGTKVA IYDMPLLVDK
     GLDRGMDLVL VVDVNVEERV RRLVEKRGLG EKDVRRRIDS QVPDEVRLKA ADVVIDNNGS
     LEDLKANMKN VIAEI