ID G0HIS4_THES4 Unreviewed; 196 AA.
AC G0HIS4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 OrderedLocusNames=GQS_04760 {ECO:0000313|EMBL:AEK72853.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK72853.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK72853.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
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; CP002920; AEK72853.1; -; Genomic_DNA.
DR RefSeq; WP_014012536.1; NC_015865.1.
DR AlphaFoldDB; G0HIS4; -.
DR STRING; 1042877.GQS_04760; -.
DR GeneID; 41609463; -.
DR KEGG; the:GQS_04760; -.
DR PATRIC; fig|1042877.9.peg.932; -.
DR eggNOG; arCOG01039; Archaea.
DR HOGENOM; CLU_119371_0_0_2; -.
DR OrthoDB; 26198at2157; -.
DR Proteomes; UP000000874; 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:AEK72853.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:AEK72853.1}.
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ SEQUENCE 196 AA; 22214 MW; CACAD026C7C2FAF2 CRC64;
MPFVVMITGI PGVGKSTITK LALKKSRAKF RLVNFGDLMF DEAVGAGLVR HRDEMRKLDP
NVQKELQMKA ARRIVEMSQR EPVLIDTHAT IRTPVGYLLG FPREVIEVIN PNFIVIIEAA
PSEILGRRLR DLKRDRDVET EEQIQRHQDL NRAAAVSYAM HSNALIKIIE NHEDKGLQEA
VHELVEVLDL AVGEYD
//
