ID   COAE_BURPS     STANDARD;      PRT;   203 AA.
AC   Q9ZF69; Q63QL2;
DT   16-OCT-2001 (Rel. 40, Created)
DT   01-FEB-2005 (Rel. 46, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Dephospho-CoA kinase (EC 2.7.1.24) (Dephosphocoenzyme A kinase).
GN   Name=coaE; OrderedLocusNames=BPSL3011;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=28450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-57.
RC   STRAIN=1026b;
RX   MEDLINE=99350433; PubMed=10419967;
RA   DeShazer D., Brett P.J., Burtnick M.N., Woods D.E.;
RT   "Molecular characterization of genetic loci required for secretion of
RT   exoproducts in Burkholderia pseudomallei.";
RL   J. Bacteriol. 181:4661-4664(1999).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of dephosphocoenzyme A to form coenzyme A (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + dephospho-CoA = ADP + CoA.
CC   -!- PATHWAY: Coenzyme A (CoA) biosynthesis; fifth (last) step.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC   -!- SIMILARITY: Belongs to the coaE family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; BX571965; CAH37022.1; -.
DR   EMBL; AF110186; AAD05190.1; -.
DR   HSSP; P44920; 1JJV.
DR   HAMAP; MF_00376; -; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   Pfam; PF01121; CoaE; 1.
DR   ProDom; PD003329; Depp_CoAkinase; 1.
DR   PROSITE; PS01294; COAE; 1.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Kinase;
KW   Transferase.
FT   NP_BIND       8     15       ATP (Potential).
SQ   SEQUENCE   203 AA;  21719 MW;  D0E6CF8FF02B9853 CRC64;
     MFSVGLTGGI GSGKTTVADL FGKLGATIVD TDLIAHRITA PQGLAMPLIA REFGAEFVAA
     DGSLDRAKMR ALVFSDESAR KRLEAITHPL IREETEREAR TAQGAYVVFV VPLLVESGTW
     KTRVDRVLVV DCDVETQIAR VTARNGFTRA QVEAIVARQA SRDARLAAAD DVIANDNASV
     AELAAEVAAL HQRYLECAAA ARN
//