COAE_THET8
ID COAE_THET8 Reviewed; 203 AA.
AC Q56416; Q5SJT2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
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, ECO:0000269|PubMed:15526298};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376, ECO:0000303|PubMed:15526298};
DE Short=DCK {ECO:0000303|PubMed:15526298};
GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=TTHA0926;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2176725; DOI=10.1016/0147-619x(90)90020-d;
RA Ashby M.K., Bergquist P.L.;
RT "Cloning and sequence of IS1000, a putative insertion sequence from Thermus
RT thermophilus HB8.";
RL Plasmid 24:1-11(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:1UF9}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15526298; DOI=10.1002/prot.20276;
RA Seto A., Murayama K., Toyama M., Ebihara A., Nakagawa N., Kuramitsu S.,
RA Shirouzu M., Yokoyama S.;
RT "ATP-induced structural change of dephosphocoenzyme A kinase from Thermus
RT thermophilus HB8.";
RL Proteins 58:235-242(2005).
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, ECO:0000269|PubMed:15526298}.
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 ECO:0000269|PubMed:15526298};
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; M33159; AAA27493.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70749.1; -; Genomic_DNA.
DR PIR; S27735; S27735.
DR RefSeq; WP_011173002.1; NC_006461.1.
DR RefSeq; YP_144192.1; NC_006461.1.
DR PDB; 1UF9; X-ray; 2.80 A; A/B/C=1-198.
DR PDBsum; 1UF9; -.
DR AlphaFoldDB; Q56416; -.
DR SMR; Q56416; -.
DR STRING; 300852.55772308; -.
DR EnsemblBacteria; BAD70749; BAD70749; BAD70749.
DR GeneID; 3169510; -.
DR KEGG; ttj:TTHA0926; -.
DR PATRIC; fig|300852.9.peg.909; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_1_1_0; -.
DR OMA; QMDIEQK; -.
DR PhylomeDB; Q56416; -.
DR UniPathway; UPA00241; UER00356.
DR EvolutionaryTrace; Q56416; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..203
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000173023"
FT DOMAIN 10..203
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 16..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15526298,
FT ECO:0007744|PDB:1UF9"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15526298,
FT ECO:0007744|PDB:1UF9"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15526298,
FT ECO:0007744|PDB:1UF9"
FT CONFLICT 182..203
FT /note="DLERALKAVLAELTGGAKGGRG -> AWKGP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1UF9"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 79..102
FT /evidence="ECO:0007829|PDB:1UF9"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1UF9"
FT TURN 114..120
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1UF9"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:1UF9"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1UF9"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:1UF9"
SQ SEQUENCE 203 AA; 22590 MW; 7CEE89F1D7D78076 CRC64;
MGHEAKHPII IGITGNIGSG KSTVAALLRS WGYPVLDLDA LAARARENKE EELKRLFPEA
VVGGRLDRRA LARLVFSDPE RLKALEAVVH PEVRRLLMEE LSRLEAPLVF LEIPLLFEKG
WEGRLHGTLL VAAPLEERVR RVMARSGLSR EEVLARERAQ MPEEEKRKRA TWVLENTGSL
EDLERALKAV LAELTGGAKG GRG
