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P27142

- KAD_GEOSE

UniProt

P27142 - KAD_GEOSE

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Protein
Adenylate kinase
Gene
adk
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism By similarity.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Temperature dependencei

Optimum temperature is 55 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMP
Binding sitei36 – 361AMP
Binding sitei92 – 921AMP
Binding sitei127 – 1271ATP
Metal bindingi130 – 1301Zinc; structural
Metal bindingi133 – 1331Zinc; structural
Metal bindingi150 – 1501Zinc; structural
Metal bindingi153 – 1531Zinc; structural
Binding sitei160 – 1601AMP
Binding sitei171 – 1711AMP
Binding sitei199 – 1991ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATPUniRule annotation
Nucleotide bindingi57 – 593AMPUniRule annotation
Nucleotide bindingi85 – 884AMPUniRule annotation
Nucleotide bindingi136 – 1372ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. adenylate kinase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. AMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKP27142.
UniPathwayiUPA00588; UER00649.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase (EC:2.7.4.3)
Short name:
AK
Alternative name(s):
ATP-AMP transphosphorylase
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Gene namesi
Name:adk
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Adenylate kinaseUniRule annotation
PRO_0000158729Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi13 – 2412
Beta strandi28 – 303
Helixi31 – 4111
Helixi44 – 5512
Helixi61 – 7212
Helixi75 – 773
Beta strandi81 – 855
Helixi90 – 10213
Beta strandi109 – 1146
Helixi117 – 1259
Beta strandi127 – 1304
Turni131 – 1333
Beta strandi136 – 1383
Turni139 – 1413
Turni151 – 1533
Beta strandi156 – 1583
Helixi161 – 1633
Helixi165 – 17915
Helixi181 – 1888
Beta strandi192 – 1965
Helixi201 – 21616

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZINX-ray1.60A1-217[»]
1ZIOX-ray1.96A1-217[»]
1ZIPX-ray1.85A1-217[»]
ProteinModelPortaliP27142.
SMRiP27142. Positions 1-217.

Miscellaneous databases

EvolutionaryTraceiP27142.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindUniRule annotation
Add
BLAST
Regioni126 – 16338LIDUniRule annotation
Add
BLAST

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27142-1 [UniParc]FASTAAdd to Basket

« Hide

MNLVLMGLPG AGKGTQAEKI VAAYGIPHIS TGDMFRAAMK EGTPLGLQAK    50
QYMDRGDLVP DEVTIGIVRE RLSKDDCQNG FLLDGFPRTV AQAEALETML 100
ADIGRKLDYV IHIDVRQDVL MERLTGRRIC RNCGATYHLI FHPPAKPGVC 150
DKCGGELYQR ADDNEATVAN RLEVNMKQMK PLVDFYEQKG YLRNINGEQD 200
MEKVFADIRE LLGGLAR 217
Length:217
Mass (Da):24,143
Last modified:August 1, 1992 - v1
Checksum:iD8701931117C53CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M88104 Genomic DNA. Translation: AAA22205.1.
PIRiB42196. KIBSAF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M88104 Genomic DNA. Translation: AAA22205.1 .
PIRi B42196. KIBSAF.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P27142.
SMRi P27142. Positions 1-217.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00588 ; UER00649 .
SABIO-RK P27142.

Miscellaneous databases

EvolutionaryTracei P27142.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
InterProi IPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
Pfami PF05191. ADK_lid. 1 hit.
[Graphical view ]
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01351. adk. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF COMPLEX WITH BI-SUBSTRATE ANALOG AP5A AND ZINC.

Entry informationi

Entry nameiKAD_GEOSE
AccessioniPrimary (citable) accession number: P27142
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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