ID   A4JBA9_BURVG            Unreviewed;       202 AA.
AC   A4JBA9;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 118.
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   OrderedLocusNames=Bcep1808_0550 {ECO:0000313|EMBL:ABO53562.1};
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO53562.1, ECO:0000313|Proteomes:UP000002287};
RN   [1] {ECO:0000313|Proteomes:UP000002287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:4I1U}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RG   Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA   Edwards T.E., Abendroth J.;
RT   "Apo crystal structure of a dephospho-CoA kinase from Burkholderia
RT   vietnamiensis.";
RL   Submitted (NOV-2012) to the PDB data bank.
RN   [3] {ECO:0007829|PDB:4I1V}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ADP.
RG   Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA   Edwards T.E., Clifton M.C., Sankaran B.;
RT   "Crystal structure of a dephospho-CoA kinase from Burkholderia
RT   vietnamiensis bound to ADP.";
RL   Submitted (NOV-2012) to the PDB data bank.
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|ARBA:ARBA00009018,
CC       ECO:0000256|HAMAP-Rule:MF_00376}.
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DR   EMBL; CP000614; ABO53562.1; -; Genomic_DNA.
DR   PDB; 4I1U; X-ray; 2.05 A; A/B=1-202.
DR   PDB; 4I1V; X-ray; 2.60 A; A/B=1-202.
DR   PDBsum; 4I1U; -.
DR   PDBsum; 4I1V; -.
DR   AlphaFoldDB; A4JBA9; -.
DR   SMR; A4JBA9; -.
DR   KEGG; bvi:Bcep1808_0550; -.
DR   eggNOG; COG0237; Bacteria.
DR   HOGENOM; CLU_057180_1_2_4; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000002287; Chromosome 1.
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   NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR   PANTHER; PTHR10695:SF46; DEPHOSPHO-COA KINASE DOMAIN-CONTAINING PROTEIN; 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 {ECO:0007829|PDB:4I1U, ECO:0007829|PDB:4I1V};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00376};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00376};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000002287};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ABO53562.1}.
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
FT   BINDING         11
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         12
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         13
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         14
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         15
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         16
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         144
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         175
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         177
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
FT   BINDING         179
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4I1V"
SQ   SEQUENCE   202 AA;  21889 MW;  EE9E620DAE950D0B CRC64;
     MYAIGLTGGI GSGKTTVADL FAARGASLVD TDLIAHRITA PAGLAMPAIE QTFGPAFVAA
     DGSLDRARMR ALIFSDEDAR RRLEAITHPL IRAETEREAR DAQGPYVIFV VPLLVESRNW
     KARCDRVLVV DCPVDTQIAR VMQRNGFTRE QVEAIIARQA TREARLAAAD DVIVNDAATP
     DALAVQVDAL HQRYLAFAAA KH
//