COAE_THEMA
ID COAE_THEMA Reviewed; 180 AA.
AC Q9X1A7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=TM_1387;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
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DR EMBL; AE000512; AAD36457.1; -; Genomic_DNA.
DR PIR; D72262; D72262.
DR RefSeq; NP_229188.1; NC_000853.1.
DR RefSeq; WP_004081589.1; NZ_CP011107.1.
DR PDB; 2GRJ; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-180.
DR PDBsum; 2GRJ; -.
DR AlphaFoldDB; Q9X1A7; -.
DR SMR; Q9X1A7; -.
DR STRING; 243274.THEMA_07390; -.
DR EnsemblBacteria; AAD36457; AAD36457; TM_1387.
DR KEGG; tma:TM1387; -.
DR eggNOG; COG0237; Bacteria.
DR InParanoid; Q9X1A7; -.
DR OMA; DVDKEYH; -.
DR OrthoDB; 1515383at2; -.
DR UniPathway; UPA00241; UER00356.
DR EvolutionaryTrace; Q9X1A7; -.
DR Proteomes; UP000008183; 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; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..180
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000173021"
FT DOMAIN 2..180
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2GRJ"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2GRJ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:2GRJ"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2GRJ"
FT TURN 107..113
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2GRJ"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:2GRJ"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2GRJ"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:2GRJ"
SQ SEQUENCE 180 AA; 20331 MW; 59321BA1139E5488 CRC64;
MVIGVTGKIG TGKSTVCEIL KNKYGAHVVN VDRIGHEVLE EVKEKLVELF GGSVLEDGKV
NRKKLAGIVF ESRENLKKLE LLVHPLMKKR VQEIINKTSG LIVIEAALLK RMGLDQLCDH
VITVVASRET ILKRNREADR RLKFQEDIVP QGIVVANNST LEDLEKKVEE VMKLVWEKRE
