ID   KAD6_METAC              Reviewed;         186 AA.
AC   Q8TJQ0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=MA_3730;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM07082.1; -; Genomic_DNA.
DR   RefSeq; WP_011023634.1; NC_003552.1.
DR   AlphaFoldDB; Q8TJQ0; -.
DR   SMR; Q8TJQ0; -.
DR   STRING; 188937.MA_3730; -.
DR   EnsemblBacteria; AAM07082; AAM07082; MA_3730.
DR   GeneID; 1475623; -.
DR   KEGG; mac:MA_3730; -.
DR   HOGENOM; CLU_079096_0_1_2; -.
DR   InParanoid; Q8TJQ0; -.
DR   OMA; QCEIFGT; -.
DR   OrthoDB; 110798at2157; -.
DR   PhylomeDB; Q8TJQ0; -.
DR   Proteomes; UP000002487; 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..186
FT                   /note="Putative adenylate kinase"
FT                   /id="PRO_0000153905"
FT   REGION          30..53
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   REGION          108..118
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         105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ   SEQUENCE   186 AA;  21160 MW;  4487C2F57D21434A CRC64;
     MLIGLTGTPG TGKTSVSKLL EKKRQWKIIH LNELIKEEHL YTEVDEKRDS VVADMELVRS
     RLPELINEME KEPANKVVIL ESHLAHYITD IVIVLRAYPP ELKKRLEKRG YSEEKVNENA
     EAESIDLILA EAFEWCDKVF EINTTGRTAE ETAGDVEKII DSLLSGKEEQ LQEYGPGSLD
     WIDSVP