P27142 (KAD_GEOSE) 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

Gene names

Name:

adk

Organism

Geobacillus stearothermophilus (Bacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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.
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 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. HAMAP MF_00235
Sequence similarities	Belongs to the adenylate kinase family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 55 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius. 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
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_0000158729

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

Helix

75 – 77

3

Beta strand

81 – 85

5

Helix

90 – 102

13

Beta strand

109 – 114

6

Helix

117 – 125

9

Beta strand

127 – 130

4

Turn

131 – 133

3

Beta strand

136 – 138

3

Turn

139 – 141

3

Turn

151 – 153

3

Beta strand

156 – 158

3

Helix

165 – 179

15

Helix

181 – 188

8

Beta strand

192 – 196

5

Helix

201 – 216

16

Sequences

	Sequence		Length	Mass (Da)
	P27142 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: D8701931117C53CF	FASTA	217	24,143
	10 20 30 40 50 60 MNLVLMGLPG AGKGTQAEKI VAAYGIPHIS TGDMFRAAMK EGTPLGLQAK QYMDRGDLVP 70 80 90 100 110 120 DEVTIGIVRE RLSKDDCQNG FLLDGFPRTV AQAEALETML ADIGRKLDYV IHIDVRQDVL 130 140 150 160 170 180 MERLTGRRIC RNCGATYHLI FHPPAKPGVC DKCGGELYQR ADDNEATVAN RLEVNMKQMK 190 200 210 PLVDFYEQKG YLRNINGEQD MEKVFADIRE LLGGLAR

References

[1]	"Zinc, a novel structural element found in the family of bacterial adenylate kinases." Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H., Barzu O., Gilles A.M. Biochemistry 31:3038-3043(1992) [PubMed: 1554691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ZINC ION.
[2]	Schiltz E., Buerkle S., Stiehle H., Mader B., Schulz G.E. Submitted (APR-1992) to the PIR data bank Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+." Berry M.B., Phillips G.N. Jr. Proteins 32:276-288(1998) [PubMed: 9715904] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR AP5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M88104 Genomic DNA. Translation: AAA22205.1.

PIR

KIBSAF. B42196.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZIN	X-ray	1.60	A	1-217	[»]
1ZIO	X-ray	1.96	A	1-217	[»]
1ZIP	X-ray	1.85	A	1-217	[»]

ProteinModelPortal

P27142.

SMR

P27142. 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...

Other

EvolutionaryTrace

P27142.

Entry information

Entry name

KAD_GEOSE

Accession

Primary (citable) accession number: P27142

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 18, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program