(data stored in ACNUC7421 zone)

SWISSPROT: B7UIF2_ECO27

ID   B7UIF2_ECO27            Unreviewed;       206 AA.
AC   B7UIF2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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   ECO:0000313|EMBL:CAS07655.1};
GN   OrderedLocusNames=E2348C_0107 {ECO:0000313|EMBL:CAS07655.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07655.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07655.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of 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
CC       (R)-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; FM180568; CAS07655.1; -; Genomic_DNA.
DR   RefSeq; WP_001269526.1; NC_011601.1.
DR   EnsemblBacteria; CAS07655; CAS07655; E2348C_0107.
DR   KEGG; ecg:E2348C_0107; -.
DR   HOGENOM; HOG000020769; -.
DR   KO; K00859; -.
DR   OMA; QMDIEQK; -.
DR   BioCyc; ECOL574521:E2348C_RS00550-MONOMER; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000008205; 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   CDD; cd02022; DPCK; 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;
DR   PRODOM; B7UIF2.
DR   SWISS-2DPAGE; B7UIF2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000256|SAAS:SAAS00779404};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:CAS07655.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000256|SAAS:SAAS00779396};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT   NP_BIND       9     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   206 AA;  22680 MW;  422C1FA06163084E CRC64;
     MRYIVALTGG IGSGKSTVAN AFADLGINVI DADIIARQVV EPGAPALHAI ADHFGANMIA
     ADGTLQRRAL RERIFANPEE KNWLNALLHP LIQQETQHQI QRATSPYVLW VVPLLVENSL
     YKKANRVLVV DVSPETQLKR TMQRDDVTRE HVEQILTAQA TREARLAVAD DVIDNNGAPD
     AIASDVARLH AHYLQLASQF VSQEKP
//

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