(data stored in ACNUC7421 zone)

SWISSPROT: COAE_ECO57

ID   COAE_ECO57              Reviewed;         206 AA.
AC   P0A6J0; P36679; P75646;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Dephospho-CoA kinase;
DE            EC=2.7.1.24;
DE   AltName: Full=Dephosphocoenzyme A kinase;
GN   Name=coaE; OrderedLocusNames=Z0113, ECs0107;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 5/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000305}.
DR   EMBL; AE005174; AAG54407.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33530.1; -; Genomic_DNA.
DR   PIR; C85493; C85493.
DR   PIR; C90642; C90642.
DR   RefSeq; NP_308134.1; NC_002695.1.
DR   RefSeq; WP_001269520.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P0A6J0; -.
DR   SMR; P0A6J0; -.
DR   STRING; 155864.Z0113; -.
DR   EnsemblBacteria; AAG54407; AAG54407; Z0113.
DR   EnsemblBacteria; BAB33530; BAB33530; BAB33530.
DR   GeneID; 913615; -.
DR   KEGG; ece:Z0113; -.
DR   KEGG; ecs:ECs0107; -.
DR   PATRIC; fig|386585.9.peg.206; -.
DR   eggNOG; ENOG4108ZQD; Bacteria.
DR   eggNOG; COG0237; LUCA.
DR   HOGENOM; HOG000020769; -.
DR   KO; K00859; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
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; P0A6J0.
DR   SWISS-2DPAGE; P0A6J0.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    206       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000172941.
FT   DOMAIN        4    200       DPCK.
FT   NP_BIND       9     16       ATP. {ECO:0000255}.
SQ   SEQUENCE   206 AA;  22622 MW;  41C69353B4EFF871 CRC64;
     MRYIVALTGG IGSGKSTVAN AFADLGINVI DADIIARQVV EPGAPALHAI ADHFGANMIA
     ADGTLQRRAL RERIFANPEE KNWLNALLHP LIQQETQHQI QQATSPYVLW VVPLLVENSL
     YKKANRVLVV DVSPETQLKR TMQRDDVTRE HVEQILAAQA TREARLAVAD DVIDNNGAPD
     AIASDVARLH AHYLQLASQF VSQEKP
//

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