KADA_SACS2
ID KADA_SACS2 Reviewed; 195 AA.
AC Q9UX83; Q53VM8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
GN Name=adkA; OrderedLocusNames=SSO0694; ORFNames=C10_036;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14; 34-47; 65-84;
RP 119-127; 136-147 AND 175-192, SUBUNIT STRUCTURE, AND CHARACTERIZATION.
RC STRAIN=ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1;
RX PubMed=12450122; DOI=10.1271/bbb.66.2112;
RA Okajima T., Kitaguchi D., Fujii K., Matsuoka H., Goto S., Uchiyama S.,
RA Kobayashi Y., Tanizawa K.;
RT "Novel trimeric adenylate kinase from an extremely thermoacidophilic
RT archaeon, Sulfolobus solfataricus: molecular cloning, nucleotide
RT sequencing, expression in Escherichia coli, and characterization of the
RT recombinant enzyme.";
RL Biosci. Biotechnol. Biochem. 66:2112-2124(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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 -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12450122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000305}.
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DR EMBL; AB006440; BAD95988.1; -; Genomic_DNA.
DR EMBL; Y18930; CAB57609.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40995.1; -; Genomic_DNA.
DR PIR; D90217; D90217.
DR PIR; JC7902; JC7902.
DR RefSeq; WP_009991247.1; NC_002754.1.
DR AlphaFoldDB; Q9UX83; -.
DR SMR; Q9UX83; -.
DR STRING; 273057.SSO0694; -.
DR EnsemblBacteria; AAK40995; AAK40995; SSO0694.
DR GeneID; 44129693; -.
DR KEGG; sso:SSO0694; -.
DR PATRIC; fig|273057.12.peg.694; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR InParanoid; Q9UX83; -.
DR OMA; HRDEMRK; -.
DR PhylomeDB; Q9UX83; -.
DR BRENDA; 2.7.4.3; 6163.
DR Proteomes; UP000001974; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="Adenylate kinase"
FT /id="PRO_0000131826"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="A -> R (in Ref. 1; BAD95988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21326 MW; 4E293837D8492D3C CRC64;
MKIGIVTGIP GVGKTTVLSF ADKILTEKGI SHKIVNYGDY MLNTALKEGY VKSRDEIRKL
QIEKQRELQA LAARRIVEDL SLLGDEGIGL IDTHAVIRTP AGYLPGLPRH VIEVLSPKVI
FLLEADPKII LERQKRDSSR ARTDYSDTAV INEVIQFARY SAMASAVLVG ASVKVVVNQE
GDPSIAASEI INSLM