ID COAE_LEGPH Reviewed; 201 AA.
AC Q5ZVH3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 27-MAR-2024, entry version 110.
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}; OrderedLocusNames=lpg1467;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU27549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017354; AAU27549.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_016356910.1; NC_002942.5.
DR RefSeq; YP_095496.1; NC_002942.5.
DR PDB; 4TTP; X-ray; 2.20 A; A=1-201.
DR PDB; 4TTQ; X-ray; 2.20 A; A=1-201.
DR PDB; 4TTR; X-ray; 2.10 A; A=1-201.
DR PDBsum; 4TTP; -.
DR PDBsum; 4TTQ; -.
DR PDBsum; 4TTR; -.
DR AlphaFoldDB; Q5ZVH3; -.
DR SMR; Q5ZVH3; -.
DR STRING; 272624.lpg1467; -.
DR PaxDb; 272624-lpg1467; -.
DR GeneID; 66490599; -.
DR KEGG; lpn:lpg1467; -.
DR PATRIC; fig|272624.6.peg.1539; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_1_2_6; -.
DR OrthoDB; 9812943at2; -.
DR BRENDA; 2.7.1.24; 2943.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000609; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..201
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000243302"
FT DOMAIN 4..201
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4TTP"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:4TTR"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4TTR"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 78..101
FT /evidence="ECO:0007829|PDB:4TTR"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4TTR"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:4TTR"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4TTR"
FT HELIX 178..199
FT /evidence="ECO:0007829|PDB:4TTR"
SQ SEQUENCE 201 AA; 22868 MW; 9400B3BA52B28786 CRC64;
MVYSVGLTGN IASGKSTVAE FFSELGINVI YADKIAKELT SKNTPCYQDI ISHFGSSVVL
NNGELDRKRI RDIIFSNSNE RLWLESLLHP VIRKKIEEQL IVCTSPYCLI EIPLLFNKHH
YPYLQKVLLV IAPLESQLDR IVKRDHCTKK QALAILATQP NLEQRLEAAD DVLINESGLS
ELKAKVNKLH QKYLREAKIK Q
//
