KADA_THEGJ
ID KADA_THEGJ Reviewed; 196 AA.
AC C5A261;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00234};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00234};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00234};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00234};
GN Name=adkA {ECO:0000255|HAMAP-Rule:MF_00234}; OrderedLocusNames=TGAM_1978;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00234};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00234}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00234}.
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DR EMBL; CP001398; ACS34480.1; -; Genomic_DNA.
DR RefSeq; WP_015859584.1; NC_012804.1.
DR AlphaFoldDB; C5A261; -.
DR SMR; C5A261; -.
DR STRING; 593117.TGAM_1978; -.
DR PaxDb; C5A261; -.
DR EnsemblBacteria; ACS34480; ACS34480; TGAM_1978.
DR GeneID; 7987035; -.
DR KEGG; tga:TGAM_1978; -.
DR PATRIC; fig|593117.10.peg.1988; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR OMA; HRDEMRK; -.
DR OrthoDB; 79684at2157; -.
DR Proteomes; UP000001488; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..196
FT /note="Adenylate kinase"
FT /id="PRO_1000204396"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00234"
SQ SEQUENCE 196 AA; 22460 MW; 51FCFE91E7EEBFAA CRC64;
MPFVVMITGI PGVGKSTITR LALKRTAINF RLVNFGDLMF EEAVKQGLVK HRDEMRKLDP
MVQKQLQLRA AQRIVEIARD EPVLLDTHAT IRTPMGYLLG FPKEVIETIR PNFIVIIEAT
PSEILGRRLR DLKRDRDVET EEQIQRHQDL NRAAAISYAM HSDALIKIIE NHEDKGLEEA
VNELVQVLNL AVREYD