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Protein

Adenylate kinase

Gene

adk

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Pathwayi: AMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from ADP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenylate kinase (adk)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from ADP, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMPUniRule annotation
Binding sitei36 – 361AMPUniRule annotation
Binding sitei92 – 921AMPUniRule annotation
Binding sitei127 – 1271ATPUniRule annotation
Binding sitei129 – 1291AMPUniRule annotation
Binding sitei140 – 1401AMPUniRule annotation
Binding sitei166 – 1661ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATPUniRule annotation
Nucleotide bindingi57 – 593AMPUniRule annotation
Nucleotide bindingi85 – 884AMPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-1484-MONOMER.
UniPathwayiUPA00588; UER00649.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AKUniRule annotation
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Gene namesi
Name:adkUniRule annotation
Ordered Locus Names:MSMEG_1484, MSMEI_1448
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Adenylate kinasePRO_1000058855Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi246196.MSMEG_1484.

Structurei

3D structure databases

ProteinModelPortaliA0QSH8.
SMRiA0QSH8. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindUniRule annotationAdd
BLAST
Regioni126 – 1327LIDUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CC8. Bacteria.
COG0563. LUCA.
HOGENOMiHOG000238772.
KOiK00939.
OMAiRIDQADC.
OrthoDBiEOG679TH4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0QSH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVVLLGPPG AGKGTQAEKL SEKLGIPQIS TGDLFRKNIG DGTPLGLEAK
60 70 80 90 100
RYLDAGDLVP AELTNRLVED RIDQPDAAEG FILDGYPRSV EQAGALKDML
110 120 130 140 150
AARNTKLDAV LEFQVSEDEL LTRLKGRGRA DDTDEVIRNR MKVYREETEP
160 170 180
LLEYYRDDLK TVNAVGALDE VFARALSALG Q
Length:181
Mass (Da):19,871
Last modified:January 9, 2007 - v1
Checksum:i7FC35CA267102844
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK75327.1.
CP001663 Genomic DNA. Translation: AFP37921.1.
RefSeqiWP_003892871.1. NZ_CP009494.1.
YP_885866.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK75327; ABK75327; MSMEG_1484.
AFP37921; AFP37921; MSMEI_1448.
GeneIDi4531206.
KEGGimsb:LJ00_07415.
msg:MSMEI_1448.
msm:MSMEG_1484.
PATRICi18075425. VBIMycSme59918_1469.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK75327.1.
CP001663 Genomic DNA. Translation: AFP37921.1.
RefSeqiWP_003892871.1. NZ_CP009494.1.
YP_885866.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0QSH8.
SMRiA0QSH8. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_1484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK75327; ABK75327; MSMEG_1484.
AFP37921; AFP37921; MSMEI_1448.
GeneIDi4531206.
KEGGimsb:LJ00_07415.
msg:MSMEI_1448.
msm:MSMEG_1484.
PATRICi18075425. VBIMycSme59918_1469.

Phylogenomic databases

eggNOGiENOG4105CC8. Bacteria.
COG0563. LUCA.
HOGENOMiHOG000238772.
KOiK00939.
OMAiRIDQADC.
OrthoDBiEOG679TH4.

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.
BioCyciMSME246196:GJ4Y-1484-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 700084 / mc(2)155.

Entry informationi

Entry nameiKAD_MYCS2
AccessioniPrimary (citable) accession number: A0QSH8
Secondary accession number(s): I7G444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 69 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.