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UniProtKB/Swiss-Prot entry Q892J5

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

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Entry information
Entry name COAE_CLOTE
Primary accession number Q892J5
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 34)
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: CTC_02101
From
Clostridium tetani [TaxID: 1513] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Massachusetts / E88;
DOI=10.1073/pnas.0335853100; PubMed=12552129 [NCBI, ExPASy, EBI, Israel, Japan]
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
"The genome sequence of Clostridium tetani, the causative agent of tetanus disease.";
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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
AE015927; AAO36600.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_782663.1; -.
3D structure databases
HSSP P36679; 1N3B. [HSSP ENTRY / PDB]
ModBase Q892J5.
Enzyme and pathway databases
BioCyc CTET212717:CTC_02101-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).
BLOCKS Q892J5.
ProtoNet Q892J5.
Genome annotation databases
GeneID 1060263; -.
GenomeReviews AE015927_GR; CTC_02101.
KEGG ctc:CTC02101; -.
NMPDR fig|212717.1.peg.1885; -.
Phylogenomic databases
HOGENOM Q892J5; -.
Genome annotation databases
CMR Q892J5; CTC_02101.
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   227  227     Dephospho-CoA kinase. PRO_0000172932
DOMAIN   31   227  197     DPCK. 
NP_BIND   36    43  8     ATP (Potential). 
Sequence information
Length: 227 AA [This is the length of the unprocessed precursor] Molecular weight: 26611 Da [This is the MW of the unprocessed precursor] CRC64: E8E4856A0ACCC060 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKEKIGMMLS DVDLEWLKKK YCIKNKGKFL KIGLTGGIGS GKSTISKMFK NMGIDVIDAD 

        70         80         90        100        110        120 
KIAREVLEKY PPILEYIEEN FGEQYIDEFG NLNRREFGNH IFSISKKERE KYENIIIPYI 

       130        140        150        160        170        180 
KLEIENQFKL YEKIGKKVCL LDAPLLIEQD MQKDLDFTVL SWVNKETQIK RVGIRDNLSE 

       190        200        210        220 
DEILNRIEAQ ISLDKKRELV DFIIDNSNTI EETRVQVEKL FQFINCL
Q892J5 in FASTA format

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