KAD_PYRAB
ID KAD_PYRAB Reviewed; 220 AA.
AC Q9UZN1; G8ZJS0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; Synonyms=adkE;
GN OrderedLocusNames=PYRAB11150; ORFNames=PAB0739;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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_00235};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. Some bacteria have evolved a zinc-coordinating structure
CC that stabilizes the LID domain. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; AJ248286; CAB50026.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70529.1; -; Genomic_DNA.
DR PIR; E75090; E75090.
DR RefSeq; WP_010868233.1; NC_000868.1.
DR AlphaFoldDB; Q9UZN1; -.
DR SMR; Q9UZN1; -.
DR STRING; 272844.PAB0739; -.
DR EnsemblBacteria; CAB50026; CAB50026; PAB0739.
DR GeneID; 1496474; -.
DR KEGG; pab:PAB0739; -.
DR PATRIC; fig|272844.11.peg.1172; -.
DR eggNOG; arCOG01046; Archaea.
DR HOGENOM; CLU_032354_1_2_2; -.
DR OMA; FHNRMRV; -.
DR OrthoDB; 55175at2157; -.
DR PhylomeDB; Q9UZN1; -.
DR UniPathway; UPA00588; UER00649.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..220
FT /note="Adenylate kinase"
FT /id="PRO_0000158901"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT REGION 124..161
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 57..59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 83..86
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 90
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 134..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 158
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 169
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
SQ SEQUENCE 220 AA; 25553 MW; 64ACCEA80FEA0535 CRC64;
MNILIFGPPG SGKSTQARRI TERYGLTYIA SGDIIRAEIK ARTPLGIEME RYLSRGDLIP
DTIVNTLIIS KLRRVRENFI MDGYPRTPEQ VITLENYLYD HGIKLDVAID IYITKEESVR
RISGRRICSK CGAVYHVEFN PPKVPGKCDI CGGELIQRPD DRPEIVEKRY DIYSKNMEPI
IKFYQKQGIY VRIDGHGSID EVWERIRPLL DYIYNQENRR
