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Q9ZCS6 (KAD_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:adk
Ordered Locus Names:RP638
OrganismRickettsia prowazekii (strain Madrid E)
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

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. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth By similarity. HAMAP MF_00235

Catalytic activity

ATP + AMP = 2 ADP. HAMAP MF_00235

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. HAMAP MF_00235

Subunit structure

Monomer By similarity. HAMAP MF_00235

Subcellular location

Cytoplasm By similarity HAMAP MF_00235.

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 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
Reference proteome
Gene Ontology (GO)
   Biological processnucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Adenylate kinase HAMAP MF_00235
PRO_0000158839

Regions

Nucleotide binding7 – 159ATP By similarity
Nucleotide binding31 – 5929AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZCS6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 23CBD806A1BEEC19

FASTA21324,504
        10         20         30         40         50         60 
MIVIFLGPPG AGKGTQGKKI AKKIDLPHIA VGDIFRTIIK TSTSEAELIN NYVKQGALIP 

        70         80         90        100        110        120 
NEIVNQVIKV FLLSSKYKNG YILDGYPRNL EQAKFFEAFI QKPQIKIIYF DVADELLIKR 

       130        140        150        160        170        180 
VLGRYSCKNC GKIYNIHFLQ PKIEHVCDVC SSSVFDYRKD DNKEVIKKRI KVYKTETYPL 

       190        200        210 
IDYYKNSGNF YIVNANKNEQ EIENDIQKIL KIN 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed: 9823893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235272 Genomic DNA. Translation: CAA15078.1.
PIRD71669.
RefSeqNP_221002.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZCS6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID883602.
GenomeReviewsGene locus RP638 in contig AJ235269_GR.
KEGGrpr:RP638.
PATRIC17902103. VBIRicPro72556_0660.

Phylogenomic databases

HOGENOMHBG630208.
OMAVLGRYSC.
ProtClustDBPRK00279.

Enzyme and pathway databases

BioCycRPRO272947:RP638-MONOMER.

Family and domain databases

HAMAPMF_00235. Adenylate_kinase_Adk.
[Tree]
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]
KOK00939.
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF57774. Adenylate_kinase_Znf_lid. 1 hit.
TIGRFAMsTIGR01351. Adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAD_RICPR
AccessionPrimary (citable) accession number: Q9ZCS6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families