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KAD6_SULTO
ID   KAD6_SULTO              Reviewed;         188 AA.
AC   Q976L5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=STK_01760;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAB65132.1; -; Genomic_DNA.
DR   RefSeq; WP_010978114.1; NC_003106.2.
DR   AlphaFoldDB; Q976L5; -.
DR   SMR; Q976L5; -.
DR   STRING; 273063.STK_01760; -.
DR   EnsemblBacteria; BAB65132; BAB65132; STK_01760.
DR   GeneID; 1458058; -.
DR   KEGG; sto:STK_01760; -.
DR   PATRIC; fig|273063.9.peg.215; -.
DR   eggNOG; arCOG01038; Archaea.
DR   OMA; QCEIFGT; -.
DR   OrthoDB; 110798at2157; -.
DR   Proteomes; UP000001015; 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; Reference proteome; Transferase.
FT   CHAIN           1..188
FT                   /note="Putative adenylate kinase"
FT                   /id="PRO_0000153916"
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   188 AA;  21342 MW;  FF35326118410B89 CRC64;
     MIIIITGTPG SGKSTIVDLL SKKLGFEKLH VSSFLIQNKA FSEYDELRQS YVIDEEKAFQ
     LIDSFIKDKN VVIETIYPSL ISHADKVIVL RKDPRVLYTE LKRRGWGELK IAENVMAEIL
     GVISGEAKEY FGNICEINVT NKKPEEVVEQ ILSNNCDNVD WLNIEEIQDL LISLDKVISS
     YEDSISDE
 
 
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