SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q92GY7

- KAD_RICCN

UniProt

Q92GY7 - KAD_RICCN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Adenylate kinase

Gene
adk, RC0985
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361AMP By similarity
Binding sitei92 – 921AMP By similarity
Binding sitei123 – 1231ATP By similarity
Metal bindingi126 – 1261Zinc; structural By similarity
Metal bindingi129 – 1291Zinc; structural By similarity
Metal bindingi146 – 1461Zinc; structural By similarity
Metal bindingi149 – 1491Zinc; structural By similarity
Binding sitei157 – 1571AMP By similarity
Binding sitei168 – 1681AMP By similarity
Binding sitei196 – 1961ATP; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATP By similarity
Nucleotide bindingi57 – 593AMP By similarity
Nucleotide bindingi85 – 884AMP By similarity
Nucleotide bindingi132 – 1332ATP By similarity

GO - Molecular functioni

  1. adenylate kinase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. AMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase (EC:2.7.4.3)
Short name:
AK
Alternative name(s):
ATP-AMP transphosphorylase
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Gene namesi
Name:adk
Ordered Locus Names:RC0985
OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
Taxonomic identifieri272944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
ProteomesiUP000000816: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Adenylate kinaseUniRule annotationPRO_0000158838Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272944.RC0985.

Structurei

3D structure databases

ProteinModelPortaliQ92GY7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbind By similarityAdd
BLAST
Regioni122 – 16039LID By similarityAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family.

Phylogenomic databases

eggNOGiCOG0563.
HOGENOMiHOG000238772.
KOiK00939.
OMAiQAKFIME.
OrthoDBiEOG679TH4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92GY7-1 [UniParc]FASTAAdd to Basket

« Hide

MMVIFLGPPG AGKGTQGKKI AKKIDLPHIA IGDIFRTIIK TSTSEAELIN    50
NYVKQGELIP NEIVNQVIKN FLLSSEYKNG YILDGYPRNL EQAKFFESFI 100
KEKIKIIYFD VSDELLIKRI LGRYSCKNCG KIYNRYFVQP KTDNVCDVCG 150
SSTFDYRKDD NEEVIKKRIE VYKTETYPLI DYYKNSGNFY IVNGSKNEQE 200
IEIDIQKILK IN 212
Length:212
Mass (Da):24,497
Last modified:December 1, 2001 - v1
Checksum:iBF785765826527A4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006914 Genomic DNA. Translation: AAL03523.1.
PIRiA97823.
RefSeqiNP_360622.1. NC_003103.1.
WP_010977577.1. NC_003103.1.

Genome annotation databases

EnsemblBacteriaiAAL03523; AAL03523; RC0985.
GeneIDi928128.
KEGGirco:RC0985.
PATRICi17889376. VBIRicCon45613_1125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006914 Genomic DNA. Translation: AAL03523.1 .
PIRi A97823.
RefSeqi NP_360622.1. NC_003103.1.
WP_010977577.1. NC_003103.1.

3D structure databases

ProteinModelPortali Q92GY7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272944.RC0985.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL03523 ; AAL03523 ; RC0985 .
GeneIDi 928128.
KEGGi rco:RC0985.
PATRICi 17889376. VBIRicCon45613_1125.

Phylogenomic databases

eggNOGi COG0563.
HOGENOMi HOG000238772.
KOi K00939.
OMAi QAKFIME.
OrthoDBi EOG679TH4.

Enzyme and pathway databases

UniPathwayi UPA00588 ; UER00649 .

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
InterProi IPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
Pfami PF05191. ADK_lid. 1 hit.
[Graphical view ]
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01351. adk. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-613 / Malish 7.

Entry informationi

Entry nameiKAD_RICCN
AccessioniPrimary (citable) accession number: Q92GY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: September 3, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Rickettsia conorii
    (strain Malish 7): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi