ID   KADA_SULIL              Reviewed;         195 AA.
AC   C3MQ83;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=LS215_1539;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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; CP001399; ACP35546.1; -; Genomic_DNA.
DR   RefSeq; WP_012711442.1; NC_012589.1.
DR   AlphaFoldDB; C3MQ83; -.
DR   SMR; C3MQ83; -.
DR   EnsemblBacteria; ACP35546; ACP35546; LS215_1539.
DR   GeneID; 7814260; -.
DR   GeneID; 7939554; -.
DR   GeneID; 8761477; -.
DR   KEGG; sis:LS215_1539; -.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OMA; HRDEMRK; -.
DR   OrthoDB; 79684at2157; -.
DR   Proteomes; UP000001747; 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..195
FT                   /note="Adenylate kinase"
FT                   /id="PRO_1000204392"
FT   BINDING         8..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00234"
SQ   SEQUENCE   195 AA;  21349 MW;  A88B4CC408F360F1 CRC64;
     MKIGIVTGIP GVGKTTVLSF ADKILTEKGI PHKIANYGDY MLNTALKEGY VNSRDEIRKL
     QIEKQRELQA LAARRIVEDL SLLGDEGIGL IDTHAVIRTP AGYLPGLPRH VIEVLSPKVI
     FLLEADPRII LERQKRDNSR ARADYSDTTV INEVIQFARY SAMASAVLVG ASVKVVINQE
     GDPSIAASDI INSLM