GenomeNet

Database: UniProt
Entry: Q6LMG7
LinkDB: Q6LMG7
Original site: Q6LMG7 
ID   COAE_PHOPR              Reviewed;         200 AA.
AC   Q6LMG7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-OCT-2014, entry version 69.
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=PBPRA3204;
OS   Photobacterium profundum (Photobacterium sp. (strain SS9)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=74109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(2005).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR378673; CAG21510.1; -; Genomic_DNA.
DR   RefSeq; YP_131312.1; NC_006370.1.
DR   ProteinModelPortal; Q6LMG7; -.
DR   STRING; 298386.PBPRA3204; -.
DR   EnsemblBacteria; CAG21510; CAG21510; PBPRA3204.
DR   GeneID; 3123331; -.
DR   KEGG; ppr:PBPRA3204; -.
DR   PATRIC; 22937473; VBIPhoPro109272_3352.
DR   eggNOG; COG0237; -.
DR   HOGENOM; HOG000020769; -.
DR   KO; K00859; -.
DR   OMA; RERVFNH; -.
DR   OrthoDB; EOG6HTP3H; -.
DR   BioCyc; PPRO298386-WGS:GSSB-3198-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; Reference proteome; Transferase.
FT   CHAIN         1    200       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000172974.
FT   DOMAIN        4    200       DPCK. {ECO:0000255|HAMAP-Rule:MF_00376}.
FT   NP_BIND       9     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   200 AA;  22058 MW;  7BFC6A0BF3014750 CRC64;
     MTMVIGLTGG IGSGKTTVAN LFGDYGIDII DADIIAREVV EPNTTGLNAI VDKLGADILL
     TDGTLDRSKL RNAIFNQQQL KDWLNGLLHP LIREKMLSNI SKATSPYCLL VVPLMVENNL
     QTMTHRLLVV DVDESVQIDR TQARDNVAPE HVKKILMAQA SRQNRNAAAD DIISNNGNSA
     ELKNKVAELH QKYIKMSHLY
//
DBGET integrated database retrieval system