P16304 (KAD_BACSU) 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
Superoxide-inducible protein 16
Short name=SOI16

Gene names

Name:	adk
Ordered Locus Names:	BSU01370

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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.
Induction	By superoxide. 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 45 degrees Celsius. Thermal denaturation midpoint (Tm) is 47.6 degrees Celsius and is raised to 66.0 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 Complete proteome Direct protein sequencing Reference proteome
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_0000158730

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 – 40

10

Helix

44 – 55

12

Helix

61 – 71

11

Helix

75 – 77

3

Beta strand

81 – 85

5

Helix

90 – 103

14

Beta strand

109 – 114

6

Helix

117 – 124

8

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

161 – 163

3

Helix

165 – 176

12

Helix

179 – 189

11

Beta strand

192 – 196

5

Helix

201 – 211

11

Sequences

	Sequence		Length	Mass (Da)
	P16304 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: ECB9ECF4F26A1E90	FASTA	217	24,119
	10 20 30 40 50 60 MNLVLMGLPG AGKGTQGERI VEDYGIPHIS TGDMFRAAMK EETPLGLEAK SYIDKGELVP 70 80 90 100 110 120 DEVTIGIVKE RLGKDDCERG FLLDGFPRTV AQAEALEEIL EEYGKPIDYV INIEVDKDVL 130 140 150 160 170 180 MERLTGRRIC SVCGTTYHLV FNPPKTPGIC DKDGGELYQR ADDNEETVSK RLEVNMKQTQ 190 200 210 PLLDFYSEKG YLANVNGQQD IQDVYADVKD LLGGLKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a Bacillus subtilis gene homologous to E. coli secY." Nakamura K., Nakamura A., Takamatsu H., Yoshikawa H., Yamane K. J. Biochem. 107:603-607(1990) [PubMed: 2113521] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic and transcriptional organization of the Bacillus subtilis spc-alpha region." Suh J.-W., Boylan S.A., Oh S.H., Price C.W. Gene 169:17-23(1996) [PubMed: 8635744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Sequence of the Bacillus subtilis spectinomycin resistance gene region." Yoshikawa H., Doi R.H. Nucleic Acids Res. 18:1647-1647(1990) [PubMed: 2139212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
[5]	"Isolation of a secY homologue from Bacillus subtilis: evidence for a common protein export pathway in eubacteria." Suh J.-W., Boylan S.A., Thomas S.M., Dolan K.M., Oliver D.B., Price C.W. Mol. Microbiol. 4:305-314(1990) [PubMed: 2110998] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99. Strain: 168.
[6]	"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: 168 / IS58.
[7]	"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: ZINC ION.
[8]	"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: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR AP5A, TEMPERATURE DEPENDENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D00619 Genomic DNA. Translation: BAA00496.1.
L47971 Genomic DNA. Translation: AAB06820.1.
AL009126 Genomic DNA. Translation: CAB11913.1.
M31102 Genomic DNA. Translation: AAB59119.1.
X51329 Genomic DNA. Translation: CAA35713.1.

PIR

JS0492.

RefSeq

NP_388018.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P3J	X-ray	1.90	A	1-217	[»]
2EU8	X-ray	1.80	A/B	1-216	[»]
2OO7	X-ray	1.80	A/B	1-217	[»]
2ORI	X-ray	1.80	A/B	1-216	[»]
2OSB	X-ray	1.80	A/B	1-216	[»]
2P3S	X-ray	1.80	A	1-217	[»]
2QAJ	X-ray	1.80	A/B	1-217	[»]
3DKV	X-ray	1.82	A	1-216	[»]
3DL0	X-ray	1.58	A/B	1-216	[»]

ProteinModelPortal

P16304.

SMR

P16304. Positions 1-216.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000003217; EBBACP00000003217; EBBACG00000003210.

GeneID

938508.

GenomeReviews

Gene locus BSU01370 in contig AL009126_GR.

KEGG

bsu:BSU01370.

NMPDR

fig|224308.1.peg.137.

PATRIC

18971783. VBIBacSub10457_0140.

Organism-specific databases

GenoList

BSU01370. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000002446.

HOGENOM

HBG630208.

OMA

VLGRYSC.

PhylomeDB

P16304.

ProtClustDB

PRK00279.

Enzyme and pathway databases

BioCyc

BSUB:BSU01370-MONOMER.

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]

KO

K00939.

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_BACSU

Accession

Primary (citable) accession number: P16304

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program