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P38372 (KAD_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:BH0155
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred 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 processNucleotide biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processAMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Adenylate kinase HAMAP-Rule MF_00235
PRO_0000158725

Regions

Nucleotide binding10 – 156ATP By similarity
Nucleotide binding57 – 593AMP By similarity
Nucleotide binding85 – 884AMP By similarity
Nucleotide binding136 – 1372ATP By similarity
Region30 – 5930NMPbind By similarity
Region126 – 16338LID By similarity

Sites

Binding site311AMP By similarity
Binding site361AMP By similarity
Binding site921AMP By similarity
Binding site1271ATP By similarity
Binding site1601AMP By similarity
Binding site1711AMP By similarity
Binding site1991ATP; via carbonyl oxygen By similarity

Experimental info

Sequence conflict41I → N in BAA01192. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P38372 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: FD5DF854B3BA3592

FASTA21724,170
        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 

« Hide

References

« Hide '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.
PIRC44859.
T44404.
RefSeqNP_241021.1. NC_002570.2.

3D structure databases

ProteinModelPortalP38372.
SMRP38372. Positions 1-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH0155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB03874; BAB03874; BAB03874.
GeneID892776.
KEGGbha:BH0155.
PATRIC18937184. VBIBacHal18977_0164.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0563.
KOK00939.
OMANEKMNAP.
OrthoDBEOG679TH4.
ProtClustDBPRK00279.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-180-MONOMER.
UniPathwayUPA00588; UER00649.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAD_BACHD
AccessionPrimary (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: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways