ID   KAD_AQUAE               Reviewed;         206 AA.
AC   O66490;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 138.
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}; OrderedLocusNames=aq_078;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG
RP   AP5A.
RX   PubMed=18026086; DOI=10.1038/nature06410;
RA   Henzler-Wildman K.A., Thai V., Lei M., Ott M., Wolf-Watz M., Fenn T.,
RA   Pozharski E., Wilson M.A., Petsko G.A., Karplus M., Hubner C.G., Kern D.;
RT   "Intrinsic motions along an enzymatic reaction trajectory.";
RL   Nature 450:838-844(2007).
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. {ECO:0000255|HAMAP-Rule:MF_00235,
CC       ECO:0000305|PubMed:18026086}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
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DR   EMBL; AE000657; AAC06438.1; -; Genomic_DNA.
DR   PIR; G70307; G70307.
DR   RefSeq; NP_213050.1; NC_000918.1.
DR   RefSeq; WP_010879988.1; NC_000918.1.
DR   PDB; 2RGX; X-ray; 1.90 A; A=1-206.
DR   PDB; 2RH5; X-ray; 2.48 A; A/B/C=1-206.
DR   PDB; 3SR0; X-ray; 1.56 A; A/B=1-206.
DR   PDB; 4CF7; X-ray; 1.59 A; A/B=1-206.
DR   PDB; 4IKE; X-ray; 1.48 A; A/B=1-206.
DR   PDB; 4JKY; X-ray; 2.37 A; A/B=1-203.
DR   PDB; 4JL5; X-ray; 1.24 A; A/B=1-203.
DR   PDB; 4JL6; X-ray; 1.65 A; A/B=1-203.
DR   PDB; 4JL8; X-ray; 1.79 A; A/B=1-203.
DR   PDB; 4JLA; X-ray; 2.12 A; A/B=1-203.
DR   PDB; 4JLB; X-ray; 1.53 A; A/B=1-203.
DR   PDB; 4JLD; X-ray; 1.55 A; A/B=1-203.
DR   PDB; 4JLO; X-ray; 1.73 A; A/B=1-203.
DR   PDB; 4JLP; X-ray; 1.43 A; A/B=1-203.
DR   PDBsum; 2RGX; -.
DR   PDBsum; 2RH5; -.
DR   PDBsum; 3SR0; -.
DR   PDBsum; 4CF7; -.
DR   PDBsum; 4IKE; -.
DR   PDBsum; 4JKY; -.
DR   PDBsum; 4JL5; -.
DR   PDBsum; 4JL6; -.
DR   PDBsum; 4JL8; -.
DR   PDBsum; 4JLA; -.
DR   PDBsum; 4JLB; -.
DR   PDBsum; 4JLD; -.
DR   PDBsum; 4JLO; -.
DR   PDBsum; 4JLP; -.
DR   AlphaFoldDB; O66490; -.
DR   SMR; O66490; -.
DR   STRING; 224324.aq_078; -.
DR   EnsemblBacteria; AAC06438; AAC06438; aq_078.
DR   KEGG; aae:aq_078; -.
DR   PATRIC; fig|224324.8.peg.68; -.
DR   eggNOG; COG0563; Bacteria.
DR   HOGENOM; CLU_032354_1_2_0; -.
DR   InParanoid; O66490; -.
DR   OrthoDB; 9805030at2; -.
DR   BRENDA; 2.7.4.3; 396.
DR   UniPathway; UPA00588; UER00649.
DR   EvolutionaryTrace; O66490; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009132; P:nucleoside diphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0009123; P:nucleoside monophosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR036193; ADK_active_lid_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01351; adk; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..206
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158718"
FT   REGION          30..59
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   REGION          123..153
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         31
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         57..59
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         82..85
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         89
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         133..134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         161
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   BINDING         189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:18026086"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           13..24
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           44..55
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           61..71
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           87..99
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          106..111
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           155..168
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           171..177
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:4JL5"
FT   HELIX           191..202
FT                   /evidence="ECO:0007829|PDB:4JL5"
SQ   SEQUENCE   206 AA;  23231 MW;  2310B49B11CBC71E CRC64;
     MILVFLGPPG AGKGTQAKRL AKEKGFVHIS TGDILREAVQ KGTPLGKKAK EYMERGELVP
     DDLIIALIEE VFPKHGNVIF DGFPRTVKQA EALDEMLEKK GLKVDHVLLF EVPDEVVIER
     LSGRRINPET GEVYHVKYNP PPPGVKVIQR EDDKPEVIKK RLEVYREQTA PLIEYYKKKG
     ILRIIDASKP VEEVYRQVLE VIGDGN
//