UniProt Accession

 KAD_ECOLI; P69441; P05082; P77123; Q2MBV3 

Genbank Protein ID

 X03038; U82664; U00096; AP009048; M38777; D90259 

Genbank Nucleotide ID

 CAA26840.1; AAB40228.1; AAC73576.1; BAE76253.1; AAA23461.1; BAA14303.1 

Protein Name

 Adenylate kinase 

Protein Synonyms/Alias

 AK; ATP-AMP transphosphorylase; ATP:AMP phosphotransferase; Adenylate monophosphate kinase 

Gene Name

 adk 

Gene Synonyms/Alias

 dnaW; plsA; b0474; JW0463 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
23	QAQFIMEKYGIPQIS	acetylation	[1]
40	DMLRAAVKSGSELGK	acetylation	[1]
47	KSGSELGKQAKDIMD	acetylation	[1]
47	KSGSELGKQAKDIMD	pupylation	[2]
50	SELGKQAKDIMDAGK	acetylation	[1]
50	SELGKQAKDIMDAGK	pupylation	[2]
57	KDIMDAGKLVTDELV	acetylation	[1]
69	ELVIALVKERIAQED	acetylation	[1]
136	SGRVYHVKFNPPKVE	acetylation	[1]
136	SGRVYHVKFNPPKVE	pupylation	[2]
141	HVKFNPPKVEGKDDV	acetylation	[1]
141	HVKFNPPKVEGKDDV	pupylation	[2]
145	NPPKVEGKDDVTGEE	acetylation	[1]
184	PLIGYYSKEAEAGNT	acetylation	[1]
192	EAEAGNTKYAKVDGT	acetylation	[1, 3]
195	AGNTKYAKVDGTKPV	acetylation	[1, 4]
200	YAKVDGTKPVAEVRA	acetylation	[1]
211	EVRADLEKILG****	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [4] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 10 15 ATP.
 NP_BIND 57 59 AMP.
 NP_BIND 85 88 AMP.
 NP_BIND 132 133 ATP.
 REGION 30 59 NMPbind.
 REGION 122 159 LID.
 BINDING 31 31 AMP.
 BINDING 36 36 AMP.
 BINDING 92 92 AMP.
 BINDING 119 119 ATP.
 BINDING 123 123 ATP.
 BINDING 156 156 AMP.
 BINDING 167 167 AMP.
 BINDING 200 200 ATP; via carbonyl oxygen.
 MOD_RES 192 192 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 214 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0004017; F:adenylate kinase activity; IDA:EcoCyc.
 GO:0016208; F:AMP binding; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0006172; P:ADP biosynthetic process; IMP:EcoliWiki.
 GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
 GO:0008654; P:phospholipid biosynthetic process; IMP:EcoliWiki.
 GO:0015951; P:purine ribonucleotide interconversion; IMP:EcoCyc.
 GO:0032774; P:RNA biosynthetic process; IMP:EcoliWiki.
 GO:0006412; P:translation; IMP:EcoliWiki. 

Interpro

 IPR006259; Adenyl_kin_sub.
 IPR000850; Adenylate_kin.
 IPR007862; Adenylate_kinase_lid-dom.
 IPR027417; P-loop_NTPase. 

Pfam

 PF00406; ADK
 PF05191; ADK_lid 

SMART

  

PROSITE

 PS00113; ADENYLATE_KINASE 

PRINTS

 PR00094; ADENYLTKNASE.