ID   KADA_METVO              Reviewed;         192 AA.
AC   P43411;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 89.
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;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
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   PROTEIN SEQUENCE OF 1-38.
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 30 to 40 degrees Celsius.;
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; U39879; AAC44865.1; -; Genomic_DNA.
DR   PDB; 1KHT; X-ray; 2.50 A; A/B/C=1-192.
DR   PDBsum; 1KHT; -.
DR   AlphaFoldDB; P43411; -.
DR   SMR; P43411; -.
DR   PRIDE; P43411; -.
DR   BRENDA; 2.7.4.3; 3268.
DR   EvolutionaryTrace; P43411; -.
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; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..192
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000131819"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        31
FT                   /note="G -> GG (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           64..82
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           107..113
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           145..166
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:1KHT"
FT   HELIX           180..191
FT                   /evidence="ECO:0007829|PDB:1KHT"
SQ   SEQUENCE   192 AA;  21303 MW;  952ABCD1788D6A8E CRC64;
     MKNKVVVVTG VPGVGSTTSS QLAMDNLRKE GVNYKMVSFG SVMFEVAKEE NLVSDRDQMR
     KMDPETQKRI QKMAGRKIAE MAKESPVAVD THSTVSTPKG YLPGLPSWVL NELNPDLIIV
     VETTGDEILM RRMSDETRVR DLDTASTIEQ HQFMNRCAAM SYGVLTGATV KIVQNRNGLL
     DQAVEELTNV LR