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Database: UniProt
Entry: P63834
LinkDB: P63834
Original site: P63834 
ID   COAE_STRP8              Reviewed;         197 AA.
AC   P63834; Q8P249;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-OCT-2014, entry version 66.
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};
GN   OrderedLocusNames=spyM18_0556;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA   Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA   Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18
RT   group A Streptococcus strains associated with acute rheumatic fever
RT   outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
CC   -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
CC       {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-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}.
CC   -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00376}.
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DR   EMBL; AE009949; AAL97252.1; -; Genomic_DNA.
DR   RefSeq; NP_606753.1; NC_003485.1.
DR   ProteinModelPortal; P63834; -.
DR   STRING; 186103.spyM18_0556; -.
DR   EnsemblBacteria; AAL97252; AAL97252; spyM18_0556.
DR   GeneID; 994922; -.
DR   KEGG; spm:spyM18_0556; -.
DR   PATRIC; 19747767; VBIStrPyo4396_0476.
DR   eggNOG; COG0237; -.
DR   HOGENOM; HOG000020768; -.
DR   KO; K00859; -.
DR   OMA; ANASDEC; -.
DR   OrthoDB; EOG6HTP3H; -.
DR   BioCyc; SPYO186103:GHJG-471-MONOMER; -.
DR   UniPathway; UPA00241; UER00356.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP.
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   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    197       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000173017.
FT   DOMAIN        2    197       DPCK. {ECO:0000255|HAMAP-Rule:MF_00376}.
FT   NP_BIND       7     14       ATP. {ECO:0000255|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   197 AA;  22074 MW;  FAF9D4ACF60E744C CRC64;
     MIIGITGGIA SGKSTVVKVI RKAGYQVIDA DQVVHDLQEK GGRLYEALRE AFGNQILKAD
     GELDRTKLSE MLFSNPDNMA TSSAIQNQII KEELAAKRDH LAQSQAIFFM DIPLLMELGY
     QDWFDAIWLV YVDAQTQLQR LMARNRLDKG KARQRIASQL PIEEKKPYAS LVIDNNGDME
     TLIKQVQSAL LSLANPR
//
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