Reviewed, UniProtKB/Swiss-Prot P43411 (KADA_METVO)

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:	adkA
Synonyms:	adk

Organism

Methanococcus voltae

Taxonomic identifier

2188 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + AMP = 2 ADP. HAMAP MF_00234
Subunit structure	Monomer Probable.
Subcellular location	Cytoplasm. HAMAP MF_00234
Sequence similarities	Belongs to the archaeal adenylate kinase family.
Biophysicochemical properties	Temperature dependence: Active from 30 to 40 degrees Celsius. HAMAP MF_00234

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
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 – 192

192

Adenylate kinase HAMAP MF_00234

PRO_0000131819

Regions

Nucleotide binding

10 – 18

9

ATP By similarity

Experimental info

Sequence conflict

31

1

G → GG AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

192

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

16 – 28

13

Turn

29 – 31

3

Beta strand

35 – 38

4

Helix

39 – 49

11

Helix

56 – 59

4

Helix

64 – 82

19

Beta strand

87 – 90

4

Beta strand

93 – 97

5

Beta strand

100 – 105

6

Helix

107 – 113

7

Beta strand

116 – 122

7

Helix

125 – 133

9

Beta strand

135 – 137

3

Beta strand

139 – 141

3

Helix

145 – 166

22

Beta strand

169 – 174

6

Helix

180 – 191

12

Sequences

	Sequence		Length	Mass (Da)
	P43411-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 952ABCD1788D6A8E	FASTA	192	21,303
	10 20 30 40 50 60 MKNKVVVVTG VPGVGSTTSS QLAMDNLRKE GVNYKMVSFG SVMFEVAKEE NLVSDRDQMR 70 80 90 100 110 120 KMDPETQKRI QKMAGRKIAE MAKESPVAVD THSTVSTPKG YLPGLPSWVL NELNPDLIIV 130 140 150 160 170 180 VETTGDEILM RRMSDETRVR DLDTASTIEQ HQFMNRCAAM SYGVLTGATV KIVQNRNGLL 190 DQAVEELTNV LR

References

[1]	"The adenylate kinase genes of M. voltae, M. thermolithotrophicus, M. jannaschii, and M. igneus define a new family of adenylate kinases." Ferber D.M., Haney P.J., Berk H., Lynn D., Konisky J. Gene 185:239-244(1997) [PubMed: 9055821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 1537 / PS.
[2]	"The adenylate kinases from a mesophilic and three thermophilic methanogenic members of the Archaea." Rusnak P., Haney P., Konisky J. J. Bacteriol. 177:2977-2981(1995) [PubMed: 7768791] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-38.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U39879 Genomic DNA. Translation: AAC44865.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KHT	X-ray	2.50	A/B/C	1-192	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.7.4.3. 20957.

Family and domain databases

HAMAP

MF_00234.
[Tree]

ProtoNet

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

Entry information

Entry name

KADA_METVO

Accession

Primary (citable) accession number: P43411

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)