ADOK_MYCTO
ID ADOK_MYCTO Reviewed; 324 AA.
AC P9WID4; L0T8X3; P83734; Q10391;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Adenosine kinase {ECO:0000250|UniProtKB:P9WID5};
DE Short=ADK {ECO:0000250|UniProtKB:P9WID5};
DE Short=AK {ECO:0000250|UniProtKB:P9WID5};
DE EC=2.7.1.20 {ECO:0000250|UniProtKB:P9WID5};
GN Name=adoK; Synonyms=cbhK; OrderedLocusNames=MT2258;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of adenosine to adenosine
CC monophosphate (AMP). Can also catalyze the phosphorylation of the
CC adenosine analog 2-methyladenosine (methyl-Ado) to methyl-AMP, the
CC first step in the metabolism of this compound to an active form that
CC displays antitubercular activity. Is not active on guanosine, inosine,
CC deoxyadenosine, cytidine, uridine, or thymidine. Prefers dGTP and GTP
CC to ATP as phosphate donors in vitro. {ECO:0000250|UniProtKB:P9WID5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20;
CC Evidence={ECO:0000250|UniProtKB:P9WID5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + GTP = AMP + GDP + H(+); Xref=Rhea:RHEA:52532,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P9WID5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + dGTP = AMP + dGDP + H(+); Xref=Rhea:RHEA:52536,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:58595,
CC ChEBI:CHEBI:61429, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P9WID5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WID5};
CC -!- ACTIVITY REGULATION: The enzyme is subject to substrate inhibition by
CC adenosine and is competitively inhibited by the adenosine analog
CC iodotubercidin. Unlike other adenosine kinases it is not stimulated by
CC inorganic phosphate. Activity is stimulated in the presence of
CC potassium. Is inhibited by a series of 7-(het)aryl-7-deazaadenine
CC ribonucleosides bearing small and bulky substituents in position 7;
CC some of them display micromolar antimycobacterial activity and low
CC cytotoxicity. {ECO:0000250|UniProtKB:P9WID5}.
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenosine: step 1/1. {ECO:0000250|UniProtKB:P9WID5}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WID5}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46544.1; -; Genomic_DNA.
DR PIR; C70785; C70785.
DR RefSeq; WP_003411414.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WID4; -.
DR SMR; P9WID4; -.
DR ChEMBL; CHEMBL4105883; -.
DR EnsemblBacteria; AAK46544; AAK46544; MT2258.
DR GeneID; 45426178; -.
DR KEGG; mtc:MT2258; -.
DR PATRIC; fig|83331.31.peg.2433; -.
DR HOGENOM; CLU_027634_5_2_11; -.
DR UniPathway; UPA00588; UER00659.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0004001; F:adenosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Nucleotide-binding; Purine salvage;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT CHAIN 2..324
FT /note="Adenosine kinase"
FT /id="PRO_0000428026"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 8
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 12
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 36
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 48
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 52
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 102
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 116
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 172..173
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 223..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
FT BINDING 257
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WID5"
SQ SEQUENCE 324 AA; 34472 MW; 0C072206A3210A1D CRC64;
MTIAVTGSIA TDHLMRFPGR FSEQLLPEHL HKVSLSFLVD DLVMHRGGVA GNMAFAIGVL
GGEVALVGAA GADFADYRDW LKARGVNCDH VLISETAHTA RFTCTTDVDM AQIASFYPGA
MSEARNIKLA DVVSAIGKPE LVIIGANDPE AMFLHTEECR KLGLAFAADP SQQLARLSGE
EIRRLVNGAA YLFTNDYEWD LLLSKTGWSE ADVMAQIDLR VTTLGPKGVD LVEPDGTTIH
VGVVPETSQT DPTGVGDAFR AGFLTGRSAG LGLERSAQLG SLVAVLVLES TGTQEWQWDY
EAAASRLAGA YGEHAAAEIV AVLA
