ID A0A0U1PUK9_9MICO Unreviewed; 205 AA.
AC A0A0U1PUK9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331};
DE Short=AK {ECO:0000256|HAMAP-Rule:MF_00235};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00235};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00235};
GN Name=adk {ECO:0000256|HAMAP-Rule:MF_00235};
GN ORFNames=C5C51_02560 {ECO:0000313|EMBL:PPI16304.1}, VT73_03810
GN {ECO:0000313|EMBL:KKM46194.1};
OS Rathayibacter toxicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM46194.1, ECO:0000313|Proteomes:UP000052979};
RN [1] {ECO:0000313|EMBL:KKM46194.1, ECO:0000313|Proteomes:UP000052979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH142 {ECO:0000313|EMBL:KKM46194.1,
RC ECO:0000313|Proteomes:UP000052979};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA 70134 or
RT CS 32), a Western Australian isolate.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPI16304.1, ECO:0000313|Proteomes:UP000237966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH99 {ECO:0000313|EMBL:PPI16304.1,
RC ECO:0000313|Proteomes:UP000237966};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP-
CC Rule:MF_00235, ECO:0000256|RuleBase:RU003331};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00235, ECO:0000256|RuleBase:RU003331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331}.
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:0000256|HAMAP-Rule:MF_00235}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|HAMAP-Rule:MF_00235,
CC ECO:0000256|RuleBase:RU003330}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00235}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKM46194.1}.
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DR EMBL; LBFI01000024; KKM46194.1; -; Genomic_DNA.
DR EMBL; PSWU01000004; PPI16304.1; -; Genomic_DNA.
DR RefSeq; WP_042733864.1; NZ_PSXN01000006.1.
DR AlphaFoldDB; A0A0U1PUK9; -.
DR STRING; 145458.APU90_03685; -.
DR GeneID; 66874910; -.
DR KEGG; rtc:APU90_03685; -.
DR PATRIC; fig|145458.8.peg.871; -.
DR eggNOG; COG0563; Bacteria.
DR OrthoDB; 9805030at2; -.
DR UniPathway; UPA00588; UER00649.
DR Proteomes; UP000052979; Unassembled WGS sequence.
DR Proteomes; UP000237966; Unassembled WGS sequence.
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; P-loop containing nucleotide triphosphate hydrolases; 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; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00235};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00235};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00235};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW Rule:MF_00235};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW ECO:0000256|RuleBase:RU003331};
KW Reference proteome {ECO:0000313|Proteomes:UP000052979};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00235}.
FT REGION 37..66
FT /note="NMP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 17..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 38
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 64..66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 92..95
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 99
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 140
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 151
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00235"
SQ SEQUENCE 205 AA; 22219 MW; 5E6AAC2A06983476 CRC64;
MNSNPVGFRL LLIGPPGAGK GTQAARLCEI LGVPAISTGD IFRANVANET EFGLQAKKYL
DAGRYVPDEL TNAIVHDRLQ EADTSTGFLL DGYPRTTEQV DELDRILAAD GNRLDAVIQL
TADPDEVVAR LIKRSAEQGR SDDTDDVIRR RLALYEEQTA PLIGLYEDRG LVVVVDGLGP
VDEVTERIVA ALEGHRVTRL DSPAA
//
