ID   KADA_METTH              Reviewed;         185 AA.
AC   O26135;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 109.
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=MTH_27;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB84536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB84536.1; ALT_INIT; Genomic_DNA.
DR   PIR; A69134; A69134.
DR   RefSeq; WP_048060730.1; NC_000916.1.
DR   AlphaFoldDB; O26135; -.
DR   SMR; O26135; -.
DR   STRING; 187420.MTH_27; -.
DR   EnsemblBacteria; AAB84536; AAB84536; MTH_27.
DR   GeneID; 1469989; -.
DR   KEGG; mth:MTH_27; -.
DR   PATRIC; fig|187420.15.peg.27; -.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OMA; HRDEMRK; -.
DR   Proteomes; UP000005223; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..185
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000131818"
FT   BINDING         8..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  20633 MW;  9B51D36F2AD5BEA9 CRC64;
     MKVVVVAGIP GSGSTTVLEN TLKELDYLNV NYGDVMLEIA VEKGLVENRD QMRTLPPEVQ
     KDIQRAAAKS IRERSLENNI IVDTHCTIKT PAGFLPGLPV WVLEELEPDM FVLVEADAEE
     IFTRRISDKT RDRDVESLQE IDLHQQMNRA AAMAYATLTG ATVKIVKNHN NQLESAVSEM
     KSVLE