KAD_FRATT
ID KAD_FRATT Reviewed; 218 AA.
AC Q5NFR4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=FTT_1161;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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 -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; AJ749949; CAG45794.1; -; Genomic_DNA.
DR RefSeq; WP_003018613.1; NZ_CP010290.1.
DR RefSeq; YP_170128.1; NC_006570.2.
DR PDB; 4PZL; X-ray; 2.10 A; A/B/C/D=1-218.
DR PDBsum; 4PZL; -.
DR AlphaFoldDB; Q5NFR4; -.
DR SMR; Q5NFR4; -.
DR STRING; 177416.FTT_1161; -.
DR DNASU; 3192396; -.
DR EnsemblBacteria; CAG45794; CAG45794; FTT_1161.
DR KEGG; ftu:FTT_1161; -.
DR eggNOG; COG0563; Bacteria.
DR OMA; FHNRMRV; -.
DR UniPathway; UPA00588; UER00649.
DR Proteomes; UP000001174; 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: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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Adenylate kinase"
FT /id="PRO_1000058832"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT REGION 122..159
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 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
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 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 132..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 156
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4PZL"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4PZL"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4PZL"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 161..183
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4PZL"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:4PZL"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:4PZL"
SQ SEQUENCE 218 AA; 24362 MW; 7314D40D15356FA2 CRC64;
MRIILLGAPG AGKGTQAKII EQKYNIAHIS TGDMIRETIK SGSALGQELK KVLDAGELVS
DEFIIKIVKD RISKNDCNNG FLLDGVPRTI PQAQELDKLG VNIDYIVEVD VADNLLIERI
TGRRIHPASG RTYHTKFNPP KVADKDDVTG EPLITRTDDN EDTVKQRLSV YHAQTAKLID
FYRNFSSTNT KIPKYIKING DQAVEKVSQD IFDQLNKR
