Reviewed, UniProtKB/Swiss-Prot Q83F01 (COAE_COXBU)

Names and origin

Protein names

Recommended name:
    Dephospho-CoA kinase
    EC=2.7.1.24
Alternative name(s):
    Dephosphocoenzyme A kinase

Gene names

Name:	coaE
Ordered Locus Names:	CBU_0152

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A By similarity.
Catalytic activity	ATP + 3'-dephospho-CoA = ADP + CoA. HAMAP MF_00376
Pathway	Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. HAMAP MF_00376
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the coaE family. Contains 1 DPCK (dephospho-CoA kinase) domain.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP dephospho-CoA kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 199	199	Dephospho-CoA kinase HAMAP MF_00376		PRO_0000172938
Regions
	Domain	3 – 199	197	DPCK
	Nucleotide binding	8 – 15	8	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q83F01-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 188F9CF995010EE1	FASTA	199	22,388
	10 20 30 40 50 60 MLRIGLTGGI GSGKSTVANY FAELGAPVID ADQIAHEITK PDQAAFKQII NHFGNAVLTK 70 80 90 100 110 120 GKFLNRTKLR ELIFENPDDR QWLENLLHPL IIAKMKTQLK KIKAPYCILA IPLLAEASQS 130 140 150 160 170 180 VDFIDRILVV DAPETLQIQR TKSRDQLSDQ QIQLILQSQS PREKRLAIAD DVIVNDQTIP 190 ILRKAVFQLH CKYLQIAQT

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016828 Genomic DNA. Translation: AAO89716.1.
RefSeq	NP_819202.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1208023.
GenomeReviews	Gene locus CBU_0152 in contig AE016828_GR.
KEGG	cbu:CBU_0152.
NMPDR	fig|227377.1.peg.146.
TIGR	CBU_0152.
Phylogenomic databases
HOGENOM	Q83F01.
OMA	IIAREVV
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0152-MON.
BRENDA	2.7.1.24. 256353.
Family and domain databases
HAMAP	MF_00376. [Tree]
InterPro	IPR001977. Depp_CoAkinase. [Graphical view]
TIGRFAMs	TIGR00152. Depp_CoAkinase. 1 hit.
PROSITE	PS51219. DPCK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COAE_COXBU

Accession

Primary (citable) accession number: Q83F01

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 24, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)