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UniProtKB/Swiss-Prot entry Q6G1B3

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

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Entry information
Entry name COAE_BARQU
Primary accession number Q6G1B3
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 30)
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: BQ00040
From
Bartonella quintana (Rochalimaea quintana) [TaxID: 803] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Toulouse;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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
BX897700; CAF25511.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_031734.1; -.
3D structure databases
ModBase Q6G1B3.
Enzyme and pathway databases
BioCyc BQUI283165:BQ00040-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 Q6G1B3.
ProtoNet Q6G1B3.
Genome annotation databases
GeneID 2867020; -.
GenomeReviews BX897700_GR; BQ00040.
KEGG bqu:BQ00040; -.
NMPDR fig|283165.1.peg.4; -.
Phylogenomic databases
HOGENOM Q6G1B3; -.
Genome annotation databases
CMR Q6G1B3; BQ00040.
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   195  195     Dephospho-CoA kinase. PRO_0000172909
DOMAIN   3   195  193     DPCK. 
NP_BIND   8    15  8     ATP (Potential). 
Sequence information
Length: 195 AA [This is the length of the unprocessed precursor] Molecular weight: 22131 Da [This is the MW of the unprocessed precursor] CRC64: 1AFE16CB6E1C34DB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKIIGLTGSI AMGKSTAADF FKQAGISVFS ADETVHQLYK SKPILSLIEH TFPGVVENGK 

        70         80         90        100        110        120 
VNRLKLSKIL INDSEKLQTL EEIIHPLVQE KEKEFIDTAR QQGKKIVVLD IPLLFEKKGE 

       130        140        150        160        170        180 
KRVDSIIVVS APLAIQKERT MTRPDMNEKK FSFINAKQMP DEKKRERADF IINTGKDLEN 

       190 
THQQVFSIIE NLLKN
Q6G1B3 in FASTA format

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