ID KADA_METJA Reviewed; 192 AA.
AC P43409;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
GN Name=adkA; Synonyms=adk; OrderedLocusNames=MJ0479;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9055821; DOI=10.1016/s0378-1119(96)00651-8;
RA Ferber D.M., Haney P.J., Berk H., Lynn D., Konisky J.;
RT "The adenylate kinase genes of M. voltae, M. thermolithotrophicus, M.
RT jannaschii, and M. igneus define a new family of adenylate kinases.";
RL Gene 185:239-244(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-30.
RX PubMed=7768791; DOI=10.1128/jb.177.11.2977-2981.1995;
RA Rusnak P., Haney P., Konisky J.;
RT "The adenylate kinases from a mesophilic and three thermophilic
RT methanogenic members of the Archaea.";
RL J. Bacteriol. 177:2977-2981(1995).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Active from 70 to 90 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U39882; AAC44863.1; -; Genomic_DNA.
DR EMBL; L77117; AAB98470.1; ALT_INIT; Genomic_DNA.
DR PIR; G64359; G64359.
DR RefSeq; WP_064496506.1; NC_000909.1.
DR AlphaFoldDB; P43409; -.
DR SMR; P43409; -.
DR STRING; 243232.MJ_0479; -.
DR PaxDb; 243232-MJ_0479; -.
DR EnsemblBacteria; AAB98470; AAB98470; MJ_0479.
DR GeneID; 1451341; -.
DR KEGG; mja:MJ_0479; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR InParanoid; P43409; -.
DR OrthoDB; 26198at2157; -.
DR PhylomeDB; P43409; -.
DR BRENDA; 2.7.4.3; 3260.
DR Proteomes; UP000000805; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13207; AAA_17; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..192
FT /note="Adenylate kinase"
FT /id="PRO_0000131814"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="S -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21772 MW; ECD533AD4C85D99E CRC64;
MKNKVVVIVG VPGVGSTTVT NKAIEELKKE GIEYKIVNFG TVMFEIAKEE GLVEHRDQLR
KLPPEEQKRI QKLAGKKIAE MAKEFNIVVD THSTIKTPKG YLPGLPAWVL EELNPDIIVL
VEAENDEILM RRLKDETRQR DFESTEDIGE HIFMNRCAAM TYAVLTGATV KIIKNRDFLL
DKAVQELIEV LK
//
