COAE_CHLPN
ID COAE_CHLPN Reviewed; 202 AA.
AC Q9Z7U3; Q9JSC9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=CPn_0611, CP_0136, CpB0635;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP98564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD18750.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38019.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98818.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98564.1; ALT_INIT; Genomic_DNA.
DR PIR; E72058; E72058.
DR PIR; H86566; H86566.
DR RefSeq; NP_224807.1; NC_000922.1.
DR RefSeq; WP_010883249.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7U3; -.
DR SMR; Q9Z7U3; -.
DR STRING; 115711.CP_0136; -.
DR PRIDE; Q9Z7U3; -.
DR EnsemblBacteria; AAD18750; AAD18750; CPn_0611.
DR EnsemblBacteria; AAF38019; AAF38019; CP_0136.
DR GeneID; 45050659; -.
DR KEGG; cpa:CP_0136; -.
DR KEGG; cpj:yacE; -.
DR KEGG; cpn:CPn_0611; -.
DR KEGG; cpt:CpB0635; -.
DR PATRIC; fig|115713.3.peg.680; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_3_1_0; -.
DR OrthoDB; 1515383at2; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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 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; Transferase.
FT CHAIN 1..202
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000172926"
FT DOMAIN 6..202
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT CONFLICT 39
FT /note="H -> N (in Ref. 3; BAA98818)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="F -> Y (in Ref. 3; BAA98818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22913 MW; EE49EE624A68F020 CRC64;
MLKLLKVSIT GDLSSGKTEA CQVFQELGAY VVSADEISHS FLIPHTRIGR RVIDLLGSDV
VVDGAFDAQA IAAKVFYNSV LLQGLEAILH PEVCRIIEEQ YHQSIQDGNY PLFVAEVPLL
YEIHYAKWFD SVILVMANED IRRERFMKKT GRSSEDFDQR CSRFLNVEEK LAQADVVVEN
NGTKKELHQK IEEYFYALKG AL
