O66490 (KAD_AQUAE) 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
Ordered Locus Names:	aq_078

Organism

Aquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Aquificaceae › Aquifex › Aquifex aeolicus

Protein attributes

Sequence length	206 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 By similarity. HAMAP-Rule MF_00235
Catalytic activity	ATP + AMP = 2 ADP. HAMAP-Rule MF_00235
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. HAMAP-Rule MF_00235
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
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 By similarity. HAMAP-Rule MF_00235
Sequence similarities	Belongs to the adenylate kinase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	AMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP adenylate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 206

206

Adenylate kinase HAMAP-Rule MF_00235

PRO_0000158718

Regions

Nucleotide binding

7 – 15

9

ATP By similarity

Nucleotide binding

31 – 59

29

AMP By similarity

Secondary structure

1

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206

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

13 – 24

12

Beta strand

27 – 30

4

Helix

31 – 41

11

Helix

44 – 55

12

Helix

61 – 71

11

Beta strand

74 – 76

3

Beta strand

78 – 82

5

Helix

87 – 99

13

Beta strand

106 – 111

6

Helix

114 – 122

9

Beta strand

124 – 126

3

Turn

128 – 130

3

Beta strand

133 – 135

3

Turn

136 – 138

3

Helix

151 – 153

3

Helix

155 – 168

14

Helix

171 – 177

7

Turn

178 – 180

3

Beta strand

182 – 186

5

Helix

191 – 202

12

Sequences

	Sequence		Length	Mass (Da)
	O66490 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 2310B49B11CBC71E	FASTA	206	23,231
	10 20 30 40 50 60 MILVFLGPPG AGKGTQAKRL AKEKGFVHIS TGDILREAVQ KGTPLGKKAK EYMERGELVP 70 80 90 100 110 120 DDLIIALIEE VFPKHGNVIF DGFPRTVKQA EALDEMLEKK GLKVDHVLLF EVPDEVVIER 130 140 150 160 170 180 LSGRRINPET GEVYHVKYNP PPPGVKVIQR EDDKPEVIKK RLEVYREQTA PLIEYYKKKG 190 200 ILRIIDASKP VEEVYRQVLE VIGDGN

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC06438.1.

PIR

G70307.

RefSeq

NP_213050.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RGX	X-ray	1.90	A	1-206	[»]
2RH5	X-ray	2.48	A/B/C	1-206	[»]
3SR0	X-ray	1.56	A/B	1-206	[»]

ProteinModelPortal

O66490.

SMR

O66490. Positions 1-203.

ModBase

Search...

Protein-protein interaction databases

STRING

224324.aq_078.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC06438; AAC06438; aq_078.

GeneID

1192503.

KEGG

aae:aq_078.

PATRIC

20957855. VBIAquAeo85532_0068.

Phylogenomic databases

eggNOG

COG0563.

HOGENOM

HOG000238772.

KO

K00939.

OMA

VVIEFRV.

ProtClustDB

CLSK2459789.

Enzyme and pathway databases

BioCyc

AAEO224324:GJBH-65-MONOMER.

UniPathway

UPA00588; UER00649.

Family and domain databases

HAMAP

MF_00235. Adenylate_kinase_Adk.

InterPro

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

PANTHER

PTHR23359. PTHR23359. 1 hit.

Pfam

PF00406. ADK. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

SUPFAM

SSF57774. Adenylate_kinase_Znf_lid. 1 hit.

TIGRFAMs

TIGR01351. adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O66490.

Entry information

Entry name

KAD_AQUAE

Accession

Primary (citable) accession number: O66490

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program