ID   KAD6_SULIL              Reviewed;         187 AA.
AC   C3MQV5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039};
DE            Short=AK {ECO:0000255|HAMAP-Rule:MF_00039};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039};
GN   OrderedLocusNames=LS215_1772;
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   -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC       catalyzes the reversible transfer of the terminal phosphate group
CC       between nucleoside triphosphates and monophosphates.
CC       {ECO:0000255|HAMAP-Rule:MF_00039}.
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_00039};
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00039}.
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DR   EMBL; CP001399; ACP35768.1; -; Genomic_DNA.
DR   RefSeq; WP_012713886.1; NC_012589.1.
DR   AlphaFoldDB; C3MQV5; -.
DR   SMR; C3MQV5; -.
DR   EnsemblBacteria; ACP35768; ACP35768; LS215_1772.
DR   GeneID; 7799409; -.
DR   KEGG; sis:LS215_1772; -.
DR   HOGENOM; CLU_079096_3_1_2; -.
DR   OMA; QCEIFGT; -.
DR   OrthoDB; 110798at2157; -.
DR   Proteomes; UP000001747; Chromosome.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12595; PTHR12595; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..187
FT                   /note="Putative adenylate kinase"
FT                   /id="PRO_1000202084"
FT   REGION          30..53
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   REGION          103..113
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ   SEQUENCE   187 AA;  21261 MW;  CC649677CBDF5938 CRC64;
     MIIIVTGTPG VGKTIASKKL SEALNLNYLS LSQFVIENKL YTEYDELRQS YIIDEDKVKE
     ELEKIISTSH LVIETIYPSL VSTADLVVVL RKNPFSLYNE LKGRGWADIK VAENVEAEIL
     GVISQEAREA FKDKVCEVDT TEMSTEQILN KILNKQCDGP IEWLVDTKVQ RFLEELDKII
     SSYENDI