ID   KADA_METMP              Reviewed;         192 AA.
AC   Q6LYG0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00234};
DE            Short=AK {ECO:0000255|HAMAP-Rule:MF_00234};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00234};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00234};
GN   Name=adkA {ECO:0000255|HAMAP-Rule:MF_00234}; OrderedLocusNames=MMP1031;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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_00234};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00234}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00234}.
CC   -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00234}.
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DR   EMBL; BX950229; CAF30587.1; -; Genomic_DNA.
DR   RefSeq; WP_011170975.1; NC_005791.1.
DR   PDB; 3H86; X-ray; 2.50 A; A/B/C/G=1-192.
DR   PDBsum; 3H86; -.
DR   AlphaFoldDB; Q6LYG0; -.
DR   SMR; Q6LYG0; -.
DR   STRING; 267377.MMP1031; -.
DR   EnsemblBacteria; CAF30587; CAF30587; MMP1031.
DR   GeneID; 41279602; -.
DR   KEGG; mmp:MMP1031; -.
DR   PATRIC; fig|267377.15.peg.1063; -.
DR   eggNOG; arCOG01039; Archaea.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OMA; HRDEMRK; -.
DR   OrthoDB; 79684at2157; -.
DR   BioCyc; MMAR267377:MMP_RS05335-MON; -.
DR   BRENDA; 2.7.4.3; 3262.
DR   EvolutionaryTrace; Q6LYG0; -.
DR   Proteomes; UP000000590; 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   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..192
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000131816"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00234"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           44..48
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           67..83
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           107..111
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           125..134
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   TURN            136..139
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           145..166
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:3H86"
FT   HELIX           180..191
FT                   /evidence="ECO:0007829|PDB:3H86"
SQ   SEQUENCE   192 AA;  21094 MW;  0899318DB158691B CRC64;
     MKNKVVVVTG VPGVGGTTVT QKAMDILSEE GLNYKMVNFG SAMFDVANEE GLASDRDQMR
     RLDPETQKRI QKMAGRKIAE MAKESPVAVD THSTVKTPKG YLPGLPAWVL TELNPDIVIV
     VETDGDEILM RRLSDESRKR DLETTASIEE HQFMNRAAAM SYGVLTGATV KIVKNKNGLV
     DNAVEELMSV LR