KAD_AQUAE
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 03-AUG-2022, entry version 133.
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; 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 OMA; FHNRMRV; -.
DR OrthoDB; 1491686at2; -.
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; -; 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 PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57774; SSF57774; 1.
DR TIGRFAMs; TIGR01351; adk; 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
