ID H1YWP2_9EURY Unreviewed; 191 AA.
AC H1YWP2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Adenylate kinase {ECO:0000256|ARBA:ARBA00019926, ECO:0000256|HAMAP-Rule:MF_00234};
DE Short=AK {ECO:0000256|HAMAP-Rule:MF_00234};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955, ECO:0000256|HAMAP-Rule:MF_00234};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|ARBA:ARBA00033336, ECO:0000256|HAMAP-Rule:MF_00234};
GN Name=adkA {ECO:0000256|HAMAP-Rule:MF_00234};
GN ORFNames=Metlim_2748 {ECO:0000313|EMBL:EHQ36783.1};
OS Methanoplanus limicola DSM 2279.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ36783.1, ECO:0000313|Proteomes:UP000005741};
RN [1] {ECO:0000313|EMBL:EHQ36783.1, ECO:0000313|Proteomes:UP000005741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ36783.1,
RC ECO:0000313|Proteomes:UP000005741};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT 2279.";
RL Submitted (OCT-2011) 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:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP-
CC Rule:MF_00234};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007088, ECO:0000256|HAMAP-Rule:MF_00234}.
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DR EMBL; CM001436; EHQ36783.1; -; Genomic_DNA.
DR RefSeq; WP_004079373.1; NZ_CM001436.1.
DR AlphaFoldDB; H1YWP2; -.
DR STRING; 937775.Metlim_2748; -.
DR PATRIC; fig|937775.9.peg.3089; -.
DR HOGENOM; CLU_119371_0_0_2; -.
DR InParanoid; H1YWP2; -.
DR OrthoDB; 26198at2157; -.
DR Proteomes; UP000005741; 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 {ECO:0000256|HAMAP-Rule:MF_00234};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:EHQ36783.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW Reference proteome {ECO:0000313|Proteomes:UP000005741};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00234}.
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ SEQUENCE 191 AA; 21468 MW; 134CFC4B589E1924 CRC64;
MSTGRKVVIT GVPGVGKTTV INASLEALKE EGINYTSINF GTCMFEVACE QENVHDRDEM
RRLDQDIQCS LQKTAAQVIA RINENVIVDT HCTVSTPSGY LAGLPAWVLN ELKPDIIVLV
ETDEDQILKR RLSDMSRQRD MEGYAAIKDH QRYNRYMAAS YSMMTGCTVK IIKNLDYLLD
NAISEMVTLL R
//
