ID   KAD6_METTH              Reviewed;         171 AA.
AC   O27656;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative adenylate kinase;
DE            Short=AK;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase;
GN   OrderedLocusNames=MTH_1619;
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   -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC       catalyzes the reversible transfer of the terminal phosphate group
CC       between nucleoside triphosphates and monophosphates. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB86092.1; -; Genomic_DNA.
DR   PIR; C69083; C69083.
DR   RefSeq; WP_010877227.1; NC_000916.1.
DR   AlphaFoldDB; O27656; -.
DR   SMR; O27656; -.
DR   STRING; 187420.MTH_1619; -.
DR   EnsemblBacteria; AAB86092; AAB86092; MTH_1619.
DR   GeneID; 1470704; -.
DR   KEGG; mth:MTH_1619; -.
DR   PATRIC; fig|187420.15.peg.1583; -.
DR   HOGENOM; CLU_079096_0_1_2; -.
DR   OMA; QCEIFGT; -.
DR   Proteomes; UP000005223; 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..171
FT                   /note="Putative adenylate kinase"
FT                   /id="PRO_0000153909"
FT   REGION          28..51
FT                   /note="NMP"
FT                   /evidence="ECO:0000250"
FT   REGION          99..109
FT                   /note="LID"
FT                   /evidence="ECO:0000250"
FT   BINDING         9..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   171 AA;  18565 MW;  AE7645A9F5087F0B CRC64;
     MICITGTPGV GKTTLAGILR ERGLEVISLG ELIRQKGFVL GRDPIRGYLE ADIEAACSHL
     QEMEGLDVVE GHLSHLCRSC SMVIVLRLHP EVLRGRLEGR GYPEGKVLEN LEAEALDVCT
     VEAFEIHGER VHEVDTTGRS PHEVADIITD IMNGSRVCPP GGVDFSGWLL G