Adenylate kinase - Mycobacterium tuberculosis

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P69440 (KAD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Adenylate kinase
Short name=AK
EC=2.7.4.3

Alternative name(s):
ATP-AMP transphosphorylase

Gene names

Name:	adk
Ordered Locus Names:	Rv0733, MT0757
ORF Names:	MTV041.07

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with GTP or UTP. Ref.3
Catalytic activity	ATP + AMP = 2 ADP. HAMAP MF_00235
Enzyme regulation	Competitively inhibited by the bisubstrate analog Ap5A, by 7-deazaadenosine 5'-monophosphate (TuMP) and 8-bromo-AMP. 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 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 is a solvent-exposed domain that is much shorter in Mycobacterium than in many other bacteria like E.coli, in which it closes over the site of phosphoryl transfer upon ATP binding. The AMP binding domain seems to play an important role in the catalysis and structural stability of the protein. HAMAP MF_00235
Sequence similarities	Belongs to the adenylate kinase family.
Biophysicochemical properties	Kinetic parameters: K_M=43 µM for ATP (at pH 7.4 and 30 degrees Celsius) Ref.3 K_M=208 µM for AMP (at pH 7.4 and 30 degrees Celsius) K_M=72 µM for ADP (at pH 7.4 and 30 degrees Celsius) V_max=235 µmol/min/mg enzyme for the forward reaction (at pH 7.4 and 30 degrees Celsius) V_max=190 µmol/min/mg enzyme for the reverse reaction (at pH 7.4 and 30 degrees Celsius) Temperature dependence: Optimum temperature is 50-55 degrees Celsius. Highly thermostable. Is half-inactivated at about 67 degrees Celsius.
Mass spectrometry	Molecular mass is 20123.5±1.6 Da from positions 1 - 181. Determined by ESI. Ref.3

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	AMP salvage Inferred from direct assay. Source: MTBBASE nucleoside triphosphate metabolic process Inferred from direct assay. Source: MTBBASE purine base metabolic process Inferred from direct assay. Source: MTBBASE
Cellular component	cytosol Inferred from direct assay. Source: MTBBASE plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	ATP binding Inferred from direct assay. Source: MTBBASE adenylate kinase activity Inferred from direct assay. Source: MTBBASE nucleoside diphosphate kinase activity Inferred from direct assay. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 181

181

Adenylate kinase HAMAP MF_00235

PRO_0000158806

Regions

Nucleotide binding

7 – 15

ATP HAMAP MF_00235

Nucleotide binding

31 – 59

AMP HAMAP MF_00235

Region

125 – 134

LID HAMAP MF_00235

Amino acid modifications

Cross-link

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) HAMAP MF_00235

Secondary structure

181

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P69440 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 8BF4829220AEEC52
Show »

FASTA

181

20,125

        10         20         30         40         50         60 
MRVLLLGPPG AGKGTQAVKL AEKLGIPQIS TGELFRRNIE EGTKLGVEAK RYLDAGDLVP 

        70         80         90        100        110        120 
SDLTNELVDD RLNNPDAANG FILDGYPRSV EQAKALHEML ERRGTDIDAV LEFRVSEEVL 

       130        140        150        160        170        180 
LERLKGRGRA DDTDDVILNR MKVYRDETAP LLEYYRDQLK TVDAVGTMDE VFARALRALG 


K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: a predictive and experimental study." Munier-Lehmann H., Burlacu-Miron S., Craescu C.T., Mantsch H.H., Schultz C.P. Proteins 36:238-248(1999) [PubMed: 10398370] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis." Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H. PLoS ONE 5:E8589-E8589(2010) [PubMed: 20066036] [Abstract] Cited for: PUPYLATION AT LYS-94, IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.
[5]	"Structural and dynamic studies on ligand-free adenylate kinase from Mycobacterium tuberculosis revealed a closed conformation that can be related to the reduced catalytic activity." Miron S., Munier-Lehmann H., Craescu C.T. Biochemistry 43:67-77(2004) [PubMed: 14705932] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842574 Genomic DNA. Translation: CAA17500.1.
AE000516 Genomic DNA. Translation: AAK44991.1.

PIR

H70822.

RefSeq

NP_215247.1. NC_000962.2.
NP_335177.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P4S	NMR	-	A	1-181	[»]
2CDN	X-ray	1.90	A	1-181	[»]

ProteinModelPortal

P69440.

SMR

P69440. Positions 1-181.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001331; EBMYCP00000001331; EBMYCG00000001331.
EBMYCT00000071398; EBMYCP00000069457; EBMYCG00000071393.

GeneID

888567.
926051.

GenomeReviews

Gene locus MT0757 in contig AE000516_GR.
Gene locus Rv0733 in contig AL123456_GR.

KEGG

mtc:MT0757.
mtu:Rv0733.

PATRIC

18123399. VBIMycTub22151_0829.

TIGR

MT0757.

Organism-specific databases

TubercuList

Rv0733.

Phylogenomic databases

GeneTree

EBGT00050000015504.

HOGENOM

HBG630208.

OMA

RADDTDE.

PhylomeDB

P69440.

ProtClustDB

PRK00279.

Family and domain databases

HAMAP

MF_00235. Adenylate_kinase_Adk.
[Tree]

InterPro

IPR000850. Adenylate_kin.
[Graphical view]

K00939.

PANTHER

PTHR23359. Adenylate_kin. 1 hit.

Pfam

PF00406. ADK. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KAD_MYCTU

Accession

Primary (citable) accession number: P69440
Secondary accession number(s): O53796, P94927

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents