ID   KADA_PYRAB              Reviewed;         196 AA.
AC   Q9V1V9; G8ZHV1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Adenylate kinase;
DE            Short=AK;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase;
GN   Name=adkA; OrderedLocusNames=PYRAB03170; ORFNames=PAB2140;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ248284; CAB49239.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69694.1; -; Genomic_DNA.
DR   PIR; H75144; H75144.
DR   RefSeq; WP_048146533.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1V9; -.
DR   SMR; Q9V1V9; -.
DR   STRING; 272844.PAB2140; -.
DR   EnsemblBacteria; CAB49239; CAB49239; PAB2140.
DR   GeneID; 1495207; -.
DR   KEGG; pab:PAB2140; -.
DR   PATRIC; fig|272844.11.peg.338; -.
DR   eggNOG; arCOG01039; Archaea.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OMA; HRDEMRK; -.
DR   OrthoDB; 79684at2157; -.
DR   PhylomeDB; Q9V1V9; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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_0000131820"
FT   BINDING         9..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   196 AA;  22286 MW;  B0D5F7554171D95D CRC64;
     MSFVVIITGI PGVGKSTITR LALQRTKAKF KLINFGDLMF EEAVKAGLVN HRDEMRKLPL
     EIQRDLQMKV AKKISEMARQ QPILLDTHAT IKTPHGYLLG LPYEVIKTLN PNFIVIIEAT
     PSEILGRRLR DLKRDRDVET EEQIQRHQDL NRAAAIAYAM HSNALIKIIE NHEDKGLEEA
     VNELVEILDL AVKEYA