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P38372

- KAD_BACHD

UniProt

P38372 - KAD_BACHD

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Protein

Adenylate kinase

Gene

adk

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMPUniRule annotation
Binding sitei36 – 361AMPUniRule annotation
Binding sitei92 – 921AMPUniRule annotation
Binding sitei127 – 1271ATPUniRule annotation
Binding sitei160 – 1601AMPUniRule annotation
Binding sitei171 – 1711AMPUniRule annotation
Binding sitei199 – 1991ATP; via carbonyl oxygenUniRule annotation

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. adenylate kinase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP

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, Nucleotide-binding

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-180-MONOMER.
UniPathwayiUPA00588; UER00649.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AKUniRule annotation
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Gene namesi
Name:adkUniRule annotation
Ordered Locus Names:BH0155
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Adenylate kinasePRO_0000158725Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi272558.BH0155.

Structurei

3D structure databases

ProteinModelPortaliP38372.
SMRiP38372. Positions 1-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563.
KOiK00939.
OMAiVLNIEVP.
OrthoDBiEOG679TH4.

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.

P38372-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLILMGLPG AGKGTQAEKI IEKYGIPHIS TGDMFRAAMK NETELGLKAK
60 70 80 90 100
SYMDAGELVP DEVTIGIVRD RLSQDDCQNG FLLDGFPRTV AQAEALEDIL
110 120 130 140 150
ASLDKKLDYV INIDVPEQLL MDRLTGRRVS PTSGRTYHVI FNPPKVEGIC
160 170 180 190 200
DVDGSELIQR DDDKPETVKK RLEVNQKQAQ PLIDFYSEKG YLQNINGDQD
210
ISRVFEDINE LLKGLSS
Length:217
Mass (Da):24,170
Last modified:December 1, 2000 - v2
Checksum:iFD5DF854B3BA3592
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41I → N in BAA01192. (PubMed:1512566)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017508 Genomic DNA. Translation: BAA75292.1.
BA000004 Genomic DNA. Translation: BAB03874.1.
D10360 Genomic DNA. Translation: BAA01192.1.
PIRiC44859.
T44404.
RefSeqiNP_241021.1. NC_002570.2.
WP_010896338.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB03874; BAB03874; BAB03874.
GeneIDi892776.
KEGGibha:BH0155.
PATRICi18937184. VBIBacHal18977_0164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017508 Genomic DNA. Translation: BAA75292.1 .
BA000004 Genomic DNA. Translation: BAB03874.1 .
D10360 Genomic DNA. Translation: BAA01192.1 .
PIRi C44859.
T44404.
RefSeqi NP_241021.1. NC_002570.2.
WP_010896338.1. NC_002570.2.

3D structure databases

ProteinModelPortali P38372.
SMRi P38372. Positions 1-216.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272558.BH0155.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB03874 ; BAB03874 ; BAB03874 .
GeneIDi 892776.
KEGGi bha:BH0155.
PATRICi 18937184. VBIBacHal18977_0164.

Phylogenomic databases

eggNOGi COG0563.
KOi K00939.
OMAi VLNIEVP.
OrthoDBi EOG679TH4.

Enzyme and pathway databases

UniPathwayi UPA00588 ; UER00649 .
BioCyci BHAL272558:GJC5-180-MONOMER.

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

« Hide 'large scale' publications
  1. "Sequence analysis of a 32-kb region including the major ribosomal protein gene clusters from alkaliphilic Bacillus sp. strain C-125."
    Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.
    Biosci. Biotechnol. Biochem. 63:452-455(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
  2. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
  3. "Molecular cloning and characterization of an alkalophilic Bacillus sp. C125 gene homologous to Bacillus subtilis secY."
    Kang S.K., Kudo T., Horikoshi K.
    J. Gen. Microbiol. 138:1365-1370(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Entry informationi

Entry nameiKAD_BACHD
AccessioniPrimary (citable) accession number: P38372
Secondary accession number(s): Q9JPW7, Q9WWJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3