KADA_METM7
ID KADA_METM7 Reviewed; 192 AA.
AC A6VFX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=MmarC7_0285;
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 -!- 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; CP000745; ABR65355.1; -; Genomic_DNA.
DR RefSeq; WP_011976692.1; NC_009637.1.
DR AlphaFoldDB; A6VFX9; -.
DR SMR; A6VFX9; -.
DR STRING; 426368.MmarC7_0285; -.
DR EnsemblBacteria; ABR65355; ABR65355; MmarC7_0285.
DR GeneID; 5327899; -.
DR KEGG; mmz:MmarC7_0285; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR OMA; HRDEMRK; -.
DR OrthoDB; 79684at2157; -.
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_1000021701"
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; 21156 MW; C391C7F94071AFD8 CRC64;
MKNKVVVVTG VPGVGGTTVT QKAMDILSEE GLNYKMVNFG SAMFEVANEE GLASDRDQMR
KLDPETQKRI QKMAGRKIAE MAKEYPVAVD THSTVKTPKG YLPGLPAWVL TELNPDMVIV
VETDGDEILM RRLSDESRKR DLETTASIEE HQFMNRAAAM SYGVLTGATV KIVKNKNGLV
DNAVEELISV LR