ID   KAD6_METM7              Reviewed;         181 AA.
AC   A6VHC3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=MmarC7_0782;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VHC3; -.
DR   SMR; A6VHC3; -.
DR   STRING; 426368.MmarC7_0782; -.
DR   EnsemblBacteria; ABR65849; ABR65849; MmarC7_0782.
DR   KEGG; mmz:MmarC7_0782; -.
DR   eggNOG; arCOG01038; Archaea.
DR   HOGENOM; CLU_079096_0_1_2; -.
DR   OMA; QCEIFGT; -.
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; Transferase.
FT   CHAIN           1..181
FT                   /note="Putative adenylate kinase"
FT                   /id="PRO_1000003092"
FT   REGION          35..58
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   REGION          106..116
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         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ   SEQUENCE   181 AA;  20633 MW;  0460D6154AAF065F CRC64;
     MIIAITGTPG VGKSTVSNLL FEKLKSGGKD IACINITEVV SKNGLYLEKD IEMDSYVVDF
     DKLNKYIQSV GTEDLILDGH VSHYLNPDYI IVLRANPLLI KNRLESRNYS SEKVKENVEA
     ELLDVCLVES IEKNDESKIF EIDCSEKDPE KIVNEILMFL DLKNPEYGNI SWLEDYFYLI
     E