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A0LIL1 (KAD_SYNFM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:Sfum_1576
OrganismSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB) [Complete proteome] [HAMAP]
Taxonomic identifier335543 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter

Protein attributes

Sequence length213 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. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain By similarity. HAMAP-Rule MF_00235

Sequence similarities

Belongs to the adenylate kinase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   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

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Adenylate kinase HAMAP-Rule MF_00235
PRO_1000021776

Regions

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

Sites

Metal binding1301Zinc; structural By similarity
Metal binding1331Zinc; structural By similarity
Metal binding1501Zinc; structural By similarity
Metal binding1531Zinc; structural By similarity
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

Sequences

Sequence LengthMass (Da)Tools
A0LIL1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 455B36B689579F3E

FASTA21323,226
        10         20         30         40         50         60 
MNIILLGPPG AGKGTQASRL IGKYAIPQIS TGDMLRAALK EGTPLGLEAK KYMDQGALVP 

        70         80         90        100        110        120 
DSVVIGLVKE RIQKPDCSKG YMLDGFPRNV SQAEALDMML GELKQRIDGV VCIEVPNKEL 

       130        140        150        160        170        180 
LGRLTGRRTC RSCGAGFHVM FDPPKTDGKC DKCGGELYQR DDDNEATVSS RLKVYEDQTK 

       190        200        210 
PLIDYYEKQG KLRRIDGVGS MDAIFGRITA ILG 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000478 Genomic DNA. Translation: ABK17263.1.
RefSeqYP_845698.1. NC_008554.1.

3D structure databases

ProteinModelPortalA0LIL1.
SMRA0LIL1. Positions 1-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335543.Sfum_1576.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK17263; ABK17263; Sfum_1576.
GeneID4460146.
KEGGsfu:Sfum_1576.
PATRIC23848531. VBISynFum78438_1839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0563.
HOGENOMHOG000238772.
KOK00939.
OMANVPFQTI.
OrthoDBEOG679TH4.
ProtClustDBCLSK2782006.

Enzyme and pathway databases

BioCycSFUM335543:GH6P-1607-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.
IPR001878. Znf_CCHC.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
SMARTSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAD_SYNFM
AccessionPrimary (citable) accession number: A0LIL1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 55 of the entry and version 1 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