ID   KADA_THESM              Reviewed;         196 AA.
AC   C6A184;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=TSIB_0313;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS89379.1; -; Genomic_DNA.
DR   RefSeq; WP_015848599.1; NC_012883.1.
DR   AlphaFoldDB; C6A184; -.
DR   SMR; C6A184; -.
DR   STRING; 604354.TSIB_0313; -.
DR   EnsemblBacteria; ACS89379; ACS89379; TSIB_0313.
DR   GeneID; 8095286; -.
DR   KEGG; tsi:TSIB_0313; -.
DR   eggNOG; arCOG01039; Archaea.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OMA; HRDEMRK; -.
DR   OrthoDB; 79684at2157; -.
DR   Proteomes; UP000009079; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..196
FT                   /note="Adenylate kinase"
FT                   /id="PRO_1000204397"
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;  22339 MW;  1F92022CFBCA8603 CRC64;
     MPFVVVITGI PGVGKSTITR LALQRTRAKF RVVNFGDIMF QEAVKAGWVS HRDEVRKLSL
     KVQRELQLKA AQRILEISQK EPVLLDTHAT IKTPLGYMLG FPREVIEVIN PRFMVIIEAN
     PSEILGRRLR DLKRDRDVET EDQIQRHQDL NRAATISYAM HSNALIKIIE NHEDKGLEEA
     VNELVKILDL AVNEDA