ID KADA_METKA Reviewed; 191 AA.
AC Q8TZB0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 95.
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=MK0025;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC Methanopyraceae; Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01242.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TZB0; -.
DR SMR; Q8TZB0; -.
DR STRING; 190192.MK0025; -.
DR PaxDb; 190192-MK0025; -.
DR EnsemblBacteria; AAM01242; AAM01242; MK0025.
DR KEGG; mka:MK0025; -.
DR PATRIC; fig|190192.8.peg.25; -.
DR HOGENOM; CLU_119371_0_0_2; -.
DR InParanoid; Q8TZB0; -.
DR OrthoDB; 26198at2157; -.
DR Proteomes; UP000001826; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13207; AAA_17; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..191
FT /note="Adenylate kinase"
FT /id="PRO_0000131815"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00234"
SQ SEQUENCE 191 AA; 21692 MW; 3A34413D4073D1EA CRC64;
MGYVIVATGV PGVGATTVTT EAVKELEGYE HVNYGDVMLE IAKEEGLVEH RDEIRKLPAE
KQREIQRLAA RRIAKMAEEK EGIIVDTHCT IKTPAGYLPG LPIWVLEELQ PDVIVLIEAD
PDEIMMRRVK DSEERQRDYD RAHEIEEHQK MNRMAAMAYA ALTGATVKII ENHDDRLEEA
VREFVETVRS L
//