P38372 (KAD_BACHD) 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

Gene names

Name:	adk
Ordered Locus Names:	BH0155

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus halodurans

Protein attributes

Sequence length	217 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. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth 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.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of three domains, a large central CORE domain and two small peripheral domains, AMP binding and LID. The LID domain closes over the site of phosphoryl transfer upon ATP binding 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
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 – 217	217	Adenylate kinase HAMAP-Rule MF_00235		PRO_0000158725
Regions
	Nucleotide binding	7 – 15	9	ATP By similarity
	Nucleotide binding	31 – 59	29	AMP By similarity
	Region	128 – 159	32	LID HAMAP-Rule MF_00235
Experimental info
	Sequence conflict	4	1	I → N in BAA01192. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P38372 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: FD5DF854B3BA3592	FASTA	217	24,170
	10 20 30 40 50 60 MNLILMGLPG AGKGTQAEKI IEKYGIPHIS TGDMFRAAMK NETELGLKAK SYMDAGELVP 70 80 90 100 110 120 DEVTIGIVRD RLSQDDCQNG FLLDGFPRTV AQAEALEDIL ASLDKKLDYV INIDVPEQLL 130 140 150 160 170 180 MDRLTGRRVS PTSGRTYHVI FNPPKVEGIC DVDGSELIQR DDDKPETVKK RLEVNQKQAQ 190 200 210 PLIDFYSEKG YLQNINGDQD ISRVFEDINE LLKGLSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 32-kb region including the major ribosomal protein gene clusters from alkaliphilic Bacillus sp. strain C-125." Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K. Biosci. Biotechnol. Biochem. 63:452-455(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[2]	"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[3]	"Molecular cloning and characterization of an alkalophilic Bacillus sp. C125 gene homologous to Bacillus subtilis secY." Kang S.K., Kudo T., Horikoshi K. J. Gen. Microbiol. 138:1365-1370(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB017508 Genomic DNA. Translation: BAA75292.1. BA000004 Genomic DNA. Translation: BAB03874.1. D10360 Genomic DNA. Translation: BAA01192.1.
PIR	C44859. T44404.
RefSeq	NP_241021.1. NC_002570.2.
3D structure databases
ProteinModelPortal	P38372.
SMR	P38372. Positions 1-216.
ModBase	Search...
Protein-protein interaction databases
STRING	272558.BH0155.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB03874; BAB03874; BAB03874.
GeneID	892776.
KEGG	bha:BH0155.
PATRIC	18937184. VBIBacHal18977_0164.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0563.
KO	K00939.
OMA	QADAMKD.
ProtClustDB	PRK00279.
Enzyme and pathway databases
BioCyc	BHAL272558:GJC5-180-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. [Graphical view]
PANTHER	PTHR23359. PTHR23359. 1 hit.
Pfam	PF00406. ADK. 1 hit. PF05191. ADK_lid. 1 hit. [Graphical view]
PRINTS	PR00094. ADENYLTKNASE.
TIGRFAMs	TIGR01351. adk. 1 hit.
PROSITE	PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KAD_BACHD

Accession

Primary (citable) accession number: P38372
Secondary accession number(s): Q9JPW7, Q9WWJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program