KAD6_THEGJ
ID KAD6_THEGJ Reviewed; 177 AA.
AC C5A628;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=TGAM_1188;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33690.1; -; Genomic_DNA.
DR RefSeq; WP_015858803.1; NC_012804.1.
DR AlphaFoldDB; C5A628; -.
DR SMR; C5A628; -.
DR STRING; 593117.TGAM_1188; -.
DR PaxDb; C5A628; -.
DR EnsemblBacteria; ACS33690; ACS33690; TGAM_1188.
DR GeneID; 7988575; -.
DR KEGG; tga:TGAM_1188; -.
DR PATRIC; fig|593117.10.peg.1187; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_1_2; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 110798at2157; -.
DR Proteomes; UP000001488; Chromosome.
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..177
FT /note="Putative adenylate kinase"
FT /id="PRO_1000202088"
FT REGION 30..50
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT REGION 99..109
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 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ SEQUENCE 177 AA; 19887 MW; 8EA61141143C577C CRC64;
MIIAVTGTPG VGKTTVSKLL AEKLGYEYVS LRDYAIEKGI GEMKGDELEV EVDELTYNFE
RDFKGKNVVV DGHLSHFLNA DLVVVLRAHP RLIGERLTER GYSREKVGEN VEAELVDVIL
VEALEENENV IEVDTTGKTP EEVVNEILEL IEKGVKKRVG VVDWSEVYDE VIPYLRL
