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Database: UniProt
Entry: A1BF55_CHLPD
LinkDB: A1BF55_CHLPD
Original site: A1BF55_CHLPD 
ID   A1BF55_CHLPD            Unreviewed;       211 AA.
AC   A1BF55;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=Cpha266_0985 {ECO:0000313|EMBL:ABL65032.1};
OS   Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL65032.1, ECO:0000313|Proteomes:UP000008701};
RN   [1] {ECO:0000313|EMBL:ABL65032.1, ECO:0000313|Proteomes:UP000008701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266 {ECO:0000313|EMBL:ABL65032.1,
RC   ECO:0000313|Proteomes:UP000008701};
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., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-2006) 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; CP000492; ABL65032.1; -; Genomic_DNA.
DR   RefSeq; WP_011744859.1; NC_008639.1.
DR   AlphaFoldDB; A1BF55; -.
DR   STRING; 290317.Cpha266_0985; -.
DR   KEGG; cph:Cpha266_0985; -.
DR   eggNOG; COG0237; Bacteria.
DR   HOGENOM; CLU_057180_3_1_10; -.
DR   OrthoDB; 9812943at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000008701; 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   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   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:ABL65032.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000008701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ABL65032.1}.
FT   BINDING         15..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   211 AA;  23296 MW;  AD3F052A7E1EFD68 CRC64;
     MVVNPFLVGV TGGIGSGKST LCRYLAELGC ELFEADVVAK ELQLDDSEVI SGIKKLFGEN
     VYGKDPEGNL FLDRRMIAGV VFSDREKLDA LNRLVHPKVF NAFDRALERA RSNGSRLLVK
     EAAILFESGS STALDFVVVV ASGMEERVAR AVAKGLGSRE EIFRRIGSQW PQEKLMEMAD
     YVVCNNGSLE ELRLKAVALY RYLLSLAERD S
//
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