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Database: UniProt
Entry: A0A0H5DQQ0_9BACT
LinkDB: A0A0H5DQQ0_9BACT
Original site: A0A0H5DQQ0_9BACT 
ID   A0A0H5DQQ0_9BACT        Unreviewed;       200 AA.
AC   A0A0H5DQQ0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ECO:0000313|EMBL:CRX38986.1};
GN   ORFNames=ELAC_1659 {ECO:0000313|EMBL:CRX38986.1};
OS   Estrella lausannensis.
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC   Estrella.
OX   NCBI_TaxID=483423 {ECO:0000313|EMBL:CRX38986.1, ECO:0000313|Proteomes:UP000220251};
RN   [1] {ECO:0000313|Proteomes:UP000220251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIB-30 {ECO:0000313|Proteomes:UP000220251};
RA   Bertelli C.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-
CC       Rule:MF_00376}.
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DR   EMBL; CWGJ01000025; CRX38986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5DQQ0; -.
DR   OrthoDB; 17745at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000220251; Unassembled WGS sequence.
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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:CRX38986.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000220251};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:CRX38986.1}.
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   200 AA;  22354 MW;  5BD1525424E20131 CRC64;
     MLKLKKIAIT GGISCGKSEF CRYLEEFGAY YVSADSIVHQ ILSPNTSLGR QVIDLLGAEV
     IDGGRIDRKK VAEKVFSTEG LLEKLEKITH PEVFKEIEHQ YEKASAEGKT SLFAAEIPLL
     FEAGGEKAFD ATIAVVAPLE KCLERYSQLP GKANDFAERM RRQLPPEEKA ERADIVIENS
     GTKDELKEKA REVYNFLTQQ
//
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