KAD_THET8
ID KAD_THET8 Reviewed; 186 AA.
AC Q5SHQ9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=TTHA1671;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RA Nakagawa N., Kondo N., Masui R., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of adenylate kinase from Thermus thermophilus HB8.";
RL Submitted (MAR-2008) to the PDB data bank.
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, ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; AP008226; BAD71494.1; -; Genomic_DNA.
DR RefSeq; WP_011173701.1; NC_006461.1.
DR RefSeq; YP_144937.1; NC_006461.1.
DR PDB; 3CM0; X-ray; 1.80 A; A=1-186.
DR PDBsum; 3CM0; -.
DR AlphaFoldDB; Q5SHQ9; -.
DR SMR; Q5SHQ9; -.
DR STRING; 300852.55773053; -.
DR EnsemblBacteria; BAD71494; BAD71494; BAD71494.
DR GeneID; 3169825; -.
DR KEGG; ttj:TTHA1671; -.
DR PATRIC; fig|300852.9.peg.1641; -.
DR eggNOG; COG0563; Bacteria.
DR HOGENOM; CLU_032354_4_1_0; -.
DR OMA; FHNRMRV; -.
DR PhylomeDB; Q5SHQ9; -.
DR UniPathway; UPA00588; UER00649.
DR EvolutionaryTrace; Q5SHQ9; -.
DR Proteomes; UP000000532; 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; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 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..186
FT /note="Adenylate kinase"
FT /id="PRO_1000058930"
FT REGION 34..63
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|Ref.2"
FT REGION 125..135
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|Ref.2"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 35
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 40
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 61..63
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 84..87
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 91
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 132
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 143
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:3CM0"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:3CM0"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:3CM0"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 137..160
FT /evidence="ECO:0007829|PDB:3CM0"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3CM0"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3CM0"
SQ SEQUENCE 186 AA; 20754 MW; 8F18FB0F47A1B7F1 CRC64;
MDVGQAVIFL GPPGAGKGTQ ASRLAQELGF KKLSTGDILR DHVARGTPLG ERVRPIMERG
DLVPDDLILE LIREELAERV IFDGFPRTLA QAEALDRLLS ETGTRLLGVV LVEVPEEELV
RRILRRAELE GRSDDNEETV RRRLEVYREK TEPLVGYYEA RGVLKRVDGL GTPDEVYARI
RAALGI
