ID   KADA_METIG              Reviewed;         192 AA.
AC   P43408;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 81.
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   Methanotorris igneus (Methanococcus igneus).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanotorris.
OX   NCBI_TaxID=2189;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 1-30.
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 70 to 90 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; U39881; AAC44862.1; -; Genomic_DNA.
DR   RefSeq; WP_013799038.1; NC_015562.1.
DR   PDB; 6PJW; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-192.
DR   PDB; 6PK5; X-ray; 2.30 A; A/B/C/D/E/F=1-192.
DR   PDB; 6PSP; X-ray; 2.25 A; A/B/C/D/E/F=1-192.
DR   PDBsum; 6PJW; -.
DR   PDBsum; 6PK5; -.
DR   PDBsum; 6PSP; -.
DR   AlphaFoldDB; P43408; -.
DR   SMR; P43408; -.
DR   GeneID; 10643737; -.
DR   OMA; HRDEMRK; -.
DR   BRENDA; 2.7.4.3; 13534.
DR   SIGNOR; P43408; -.
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_0000131813"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        8
FT                   /note="V -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="T -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           64..84
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           107..113
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           145..166
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:6PSP"
FT   HELIX           180..190
FT                   /evidence="ECO:0007829|PDB:6PSP"
SQ   SEQUENCE   192 AA;  21400 MW;  AB2EC9C9DB905E75 CRC64;
     MKNKVVVVTG VPGVGGTTLT QKTIEKLKEE GIEYKMVNFG TVMFEVAKEE GLVEDRDQMR
     KLDPDTQKRI QKLAGRKIAE MAKESNVIVD THSTVKTPKG YLAGLPIWVL EELNPDIIVI
     VETSSDEILM RRLGDATRNR DIELTSDIDE HQFMNRCAAM AYGVLTGATV KIIKNRDGLL
     DKAVEELISV LK