Q83E75 (KAD_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylate kinase
Short name=AK
EC=2.7.4.3

Alternative name(s):
ATP-AMP transphosphorylase
ATP:AMP phosphotransferase
Adenylate monophosphate kinase

Gene names

Name:	adk
Ordered Locus Names:	CBU_0454

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism By similarity. HAMAP-Rule MF_00235
Catalytic activity	ATP + AMP = 2 ADP. HAMAP-Rule MF_00235
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. HAMAP-Rule MF_00235
Subunit structure	Monomer By similarity. HAMAP-Rule MF_00235
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00235.
Domain	Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis By similarity. HAMAP-Rule MF_00235
Sequence similarities	Belongs to the adenylate kinase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	AMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP adenylate 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 – 231	231	Adenylate kinase HAMAP-Rule MF_00235		PRO_0000158763
Regions
	Nucleotide binding	12 – 17	6	ATP By similarity
	Nucleotide binding	59 – 61	3	AMP By similarity
	Nucleotide binding	87 – 90	4	AMP By similarity
	Nucleotide binding	134 – 135	2	ATP By similarity
	Region	32 – 61	30	NMPbind By similarity
	Region	124 – 161	38	LID By similarity
Sites
	Binding site	33	1	AMP By similarity
	Binding site	38	1	AMP By similarity
	Binding site	94	1	AMP By similarity
	Binding site	125	1	ATP By similarity
	Binding site	158	1	AMP By similarity
	Binding site	169	1	AMP By similarity
	Binding site	205	1	ATP; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83E75 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: C8DCA6D19E2B622D	FASTA	231	25,866
	10 20 30 40 50 60 MPLRIILLGL PGAGKGTQAD FIAKHLDIPK ISTGDMLRAA VKAKTPLGLE VKKIMESGGL 70 80 90 100 110 120 VSDEIMIALV KERVKLPDCH KGYLLDGFPR TLAQADALNA AAIKIDLVIE IDVPEEEIIE 130 140 150 160 170 180 RMTGRLIHPA SGRTYHRRYN PPKVADKDDV TGEPLIQRAD DREETVRHRL AVYRKQTSPL 190 200 210 220 230 SDYYAQWEKS GDPQAPKYFR ISGLGSMEEV RERILQVFEA YDPRDSGNLE H

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO90004.1.
RefSeq	NP_819490.1. NC_002971.3.
3D structure databases
ProteinModelPortal	Q83E75.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_0454.
Proteomic databases
PRIDE	Q83E75.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO90004; AAO90004; CBU_0454.
GeneID	1208338.
KEGG	cbu:CBU_0454.
PATRIC	17929599. VBICoxBur82552_0445.
Phylogenomic databases
eggNOG	COG0563.
HOGENOM	HOG000238772.
KO	K00939.
OMA	QADAMKD.
ProtClustDB	PRK00279.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-452-MONOMER.
UniPathway	UPA00588; UER00649.
Family and domain databases
HAMAP	MF_00235. Adenylate_kinase_Adk.
InterPro	IPR006259. Adenyl_kin_sub. IPR000850. Adenylate_kin. IPR007862. Adenylate_kinase_lid-dom. IPR027417. P-loop_NTPase. [Graphical view]
PANTHER	PTHR23359. PTHR23359. 1 hit.
Pfam	PF00406. ADK. 1 hit. PF05191. ADK_lid. 1 hit. [Graphical view]
PRINTS	PR00094. ADENYLTKNASE.
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR01351. adk. 1 hit.
PROSITE	PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KAD_COXBU

Accession

Primary (citable) accession number: Q83E75

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	May 29, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program