ID   KADA_METMJ              Reviewed;         192 AA.
AC   A3CT21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Memar_0588;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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   -!- 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; CP000562; ABN56521.1; -; Genomic_DNA.
DR   RefSeq; WP_011843431.1; NC_009051.1.
DR   AlphaFoldDB; A3CT21; -.
DR   SMR; A3CT21; -.
DR   STRING; 368407.Memar_0588; -.
DR   EnsemblBacteria; ABN56521; ABN56521; Memar_0588.
DR   GeneID; 4846523; -.
DR   KEGG; mem:Memar_0588; -.
DR   eggNOG; arCOG01039; Archaea.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OMA; HRDEMRK; -.
DR   OrthoDB; 79684at2157; -.
DR   Proteomes; UP000002146; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..192
FT                   /note="Adenylate kinase"
FT                   /id="PRO_1000021702"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00234"
SQ   SEQUENCE   192 AA;  21118 MW;  F1A0BFE865D5D427 CRC64;
     MLGKKVVVTG VPGVGKTTVI NGAMERLATE GVAYKAVNFG TFMFEVAKKE NLASDRDEMR
     KLEKDVQKRL QQAAATGIAA MSGEANIIID THSTVKTPTG FLAGLPEWVL RELMPDIVVL
     VETDPDQILM RRLGDASRAR DMEGYRAIAE HQEFNRAVSA AYAMYTGCTI KIVRNENFLL
     EQGIDDLVSV LR