P84139 (KAD_BACGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Adenylate kinase Short name=AK EC=2.7.4.3 Alternative name(s): ATP-AMP transphosphorylase
Organism	Bacillus globisporus
Taxonomic identifier	1459 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Planococcaceae › Sporosarcina

Protein attributes

Sequence length	217 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. 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. HAMAP MF_00235
Miscellaneous	The zinc ion does not participate in catalysis. It has a structural role in stabilizing the LID domain, which does not seem to be involved in directly binding DNA/RNA By similarity. HAMAP MF_00235
Sequence similarities	Belongs to the adenylate kinase family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 35 degrees Celsius. Thermal denaturation midpoint (Tm) is 43.3 degrees Celsius and is raised to 60.4 degrees Celsius when AK is complexed with the inhibitor Ap5A. HAMAP MF_00235

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 217

217

Adenylate kinase HAMAP MF_00235

PRO_0000158724

Regions

Nucleotide binding

7 – 15

9

ATP HAMAP MF_00235

Nucleotide binding

31 – 59

29

AMP HAMAP MF_00235

Region

128 – 159

32

LID HAMAP MF_00235

Sites

Metal binding

130

1

Zinc

Metal binding

133

1

Zinc

Metal binding

150

1

Zinc

Metal binding

153

1

Zinc

Secondary structure

1

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217

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

13 – 24

12

Beta strand

28 – 30

3

Helix

31 – 41

11

Helix

44 – 55

12

Helix

61 – 72

12

Beta strand

81 – 85

5

Helix

90 – 102

13

Beta strand

109 – 114

6

Helix

117 – 125

9

Beta strand

126 – 130

5

Turn

131 – 133

3

Beta strand

136 – 138

3

Turn

139 – 141

3

Turn

151 – 153

3

Beta strand

156 – 158

3

Helix

165 – 187

23

Turn

188 – 190

3

Beta strand

192 – 196

5

Helix

201 – 212

12

Sequences

	Sequence		Length	Mass (Da)
	P84139 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: A8E28D5CF7C747AE	FASTA	217	23,888
	10 20 30 40 50 60 MNIVLMGLPG AGKGTQADRI VEKYGTPHIS TGDMFRAAIQ EGTELGVKAK SFMDQGALVP 70 80 90 100 110 120 DEVTIGIVRE RLSKSDCDNG FLLDGFPRTV PQAEALDQLL ADMGRKIEHV LNIQVEKEEL 130 140 150 160 170 180 IARLTGRRIC KVCGTSYHLL FNPPQVEGKC DKDGGELYQR ADDNPDTVTN RLEVNMNQTA 190 200 210 PLLAFYDSKE VLVNINGQKD IKDVFKDLDV ILQGNGQ

References

[1]	"Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases." Bae E., Phillips G.N. Jr. J. Biol. Chem. 279:28202-28208(2004) [PubMed: 15100224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR AP5A, TEMPERATURE DEPENDENCE.
[2]	"Zinc, a structural component of adenylate kinases from Gram-positive bacteria." Gilles A.-M., Glaser P., Perrier V., Meier A., Longin R., Sebald M., Maignan L., Pistotnik E., Barzu O. J. Bacteriol. 176:520-523(1994) [PubMed: 8288548] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, ZINC ION.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S3G	X-ray	2.25	A	1-217	[»]

ProteinModelPortal

P84139.

SMR

P84139. Positions 1-217.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_00235. Adenylate_kinase_Adk.
[Tree]

InterPro

IPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]

PANTHER

PTHR23359. Adenylate_kin. 1 hit.

Pfam

PF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

TIGRFAMs

TIGR01351. Adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KAD_BACGO

Accession

Primary (citable) accession number: P84139

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	September 13, 2004
Last modified:	May 31, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program