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UniProtKB/Swiss-Prot entry Q9PMD9

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

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Entry information
Entry name COAE_CAMJE
Primary accession number Q9PMD9
Secondary accession number Q0P895
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 50)
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: Cj1530
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(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
AL111168; CAL35630.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H81299; H81299.
3D structure databases
ModBase Q9PMD9.
Protein-protein interaction databases
IntAct Q9PMD9; -.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ1530-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 Q9PMD9.
Genome annotation databases
GenomeReviews AL111168_GR; Cj1530.
KEGG cje:Cj1530; -.
CMR Q9PMD9; Cj1530.
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   201  201     Dephospho-CoA kinase. PRO_0000172922
DOMAIN   4   201  198     DPCK. 
NP_BIND   9    16  8     ATP (Potential). 
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 23048 Da [This is the MW of the unprocessed precursor] CRC64: 532D6B6C821B2608 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKNAFFVTAS IACGKSTFIE IANSLGFKSI SADKIAHKIL DENALELEKI FSPFSLKNLL 

        70         80         90        100        110        120 
KKEKKIDRKI LGEIVFNNKE AKKILENFTH PKIRAKILEQ MQILDKENKA FFVEIPLFFE 

       130        140        150        160        170        180 
SGAYENLGKV IVIYTPKELS LKRIMQRDKL SLEAAKARLD SQIDIEEKLK KADFIIKNTN 

       190        200 
SYADFRQECV KVIQEISKGN M
Q9PMD9 in FASTA format

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