KADA_THEKO
ID KADA_THEKO Reviewed; 196 AA.
AC Q5JJH2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=TK1517;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85706.1; -; Genomic_DNA.
DR RefSeq; WP_011250468.1; NC_006624.1.
DR AlphaFoldDB; Q5JJH2; -.
DR SMR; Q5JJH2; -.
DR IntAct; Q5JJH2; 1.
DR MINT; Q5JJH2; -.
DR STRING; 69014.TK1517; -.
DR EnsemblBacteria; BAD85706; BAD85706; TK1517.
DR GeneID; 3235845; -.
DR KEGG; tko:TK1517; -.
DR PATRIC; fig|69014.16.peg.1477; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR InParanoid; Q5JJH2; -.
DR OMA; HRDEMRK; -.
DR OrthoDB; 79684at2157; -.
DR PhylomeDB; Q5JJH2; -.
DR Proteomes; UP000000536; 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_0000131824"
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; 22138 MW; 7B2E7DAD153175ED CRC64;
MPFVVVITGI PGVGKSTITK LALKKTRAKF RLVNFGDLMF EEAVNMGLVK HRDEMRKLDP
LTQKELQLKV AQRIVEIARK EPVLLDTHAT IRTPAGYLLG FPREVIEILN PNFIVIIEAA
PSEILGRRLR DLKRDRDVET EEQIARHQDL NRAAAIAYAM HSNALIKIIE NHEDKGLEEA
VNELVKVLDL AVSEYA