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UniProtKB/Swiss-Prot entry Q9PJP9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COAE_CHLMU
Primary accession number Q9PJP9
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on June 1, 2001 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 53)
Name and origin of the protein
Protein name Dephospho-CoA kinase
Synonyms EC 2.7.1.24
Dephosphocoenzyme A kinase
Gene name
Name: coaE
OrderedLocusNames: TC_0779
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE002160; AAF39582.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C81665; C81665.
RefSeq NP_297152.1; -.
3D structure databases
HSSP P44920; 1JJV. [HSSP ENTRY / PDB]
ModBase Q9PJP9.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0779-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004140; Molecular function: dephospho-CoA kinase activity (inferred from electronic annotation from HAMAP).
GO:0015937; Biological process: coenzyme A biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00376; -; 1.
PBIL [Tree]
InterPro IPR001977; Depp_CoAkinase.
Graphical view of domain structure.
PANTHER PTHR10695; Depp_CoAkinase; 1.
Pfam PF01121; CoaE; 1.
Pfam graphical view of domain structure.
ProDom PD003329; Depp_CoAkinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00152; Depp_CoAkinase; 1.
PROSITE PS51219; DPCK; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9PJP9.
Genome annotation databases
GeneID 1246144; -.
GenomeReviews AE002160_GR; TC_0779.
KEGG cmu:TC0779; -.
TIGR TC_0779; -.
Phylogenomic databases
HOGENOM Q9PJP9; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   202  202     Dephospho-CoA kinase. PRO_0000172925
DOMAIN   6   202  197     DPCK. 
NP_BIND   11    18  8     ATP (Potential). 
Sequence information
Length: 202 AA [This is the length of the unprocessed precursor] Molecular weight: 22878 Da [This is the MW of the unprocessed precursor] CRC64: B31A49790EC06C17 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLDLLKISVT GDPSSGKTEA CQVFEELGAF VISADKVSHS FLVPYTSEGQ RVVDLLGPEI 

        70         80         90        100        110        120 
IVENTLNRKA IAKKVFGNRD LLLSLEKILH PGVCRFVEEN YTQVVQAQKY SLFVVEVPLL 

       130        140        150        160        170        180 
YEIQYADWFD RVILISADTE IRKERFLKKT GGSDTSFDLR CARFSSLEEK ILRADVVIEN 

       190        200 
NGTKEEFRHK VKQCFKALKG TI
Q9PJP9 in FASTA format

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