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Adenosine kinase (ADK) (AK) (EC 2.7.1.20)

 ADOK_MYCTO              Reviewed;         324 AA.
P9WID4; L0T8X3; P83734; Q10391;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-JUN-2017, entry version 21.
RecName: Full=Adenosine kinase {ECO:0000250|UniProtKB:P9WID5};
Short=ADK {ECO:0000250|UniProtKB:P9WID5};
Short=AK {ECO:0000250|UniProtKB:P9WID5};
EC=2.7.1.20 {ECO:0000250|UniProtKB:P9WID5};
Name=adoK; Synonyms=cbhK; OrderedLocusNames=MT2258;
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83331;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and
laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
-!- FUNCTION: Catalyzes the phosphorylation of adenosine to adenosine
monophosphate (AMP). Can also catalyze the phosphorylation of the
adenosine analog 2-methyladenosine (methyl-Ado) to methyl-AMP, the
first step in the metabolism of this compound to an active form
that displays antitubercular activity. Is not active on guanosine,
inosine, deoxyadenosine, cytidine, uridine, or thymidine. Prefers
dGTP and GTP to ATP as phosphate donors in vitro.
{ECO:0000250|UniProtKB:P9WID5}.
-!- CATALYTIC ACTIVITY: ATP + adenosine = ADP + AMP.
{ECO:0000250|UniProtKB:P9WID5}.
-!- CATALYTIC ACTIVITY: GTP + adenosine = GDP + AMP.
{ECO:0000250|UniProtKB:P9WID5}.
-!- CATALYTIC ACTIVITY: dGTP + adenosine = dGDP + AMP.
{ECO:0000250|UniProtKB:P9WID5}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P9WID5};
-!- ENZYME REGULATION: The enzyme is subject to substrate inhibition
by adenosine and is competitively inhibited by the adenosine
analog iodotubercidin. Unlike other adenosine kinases it is not
stimulated by inorganic phosphate. Activity is stimulated in the
presence of potassium. Is inhibited by a series of 7-(het)aryl-7-
deazaadenine ribonucleosides bearing small and bulky substituents
in position 7; some of them display micromolar antimycobacterial
activity and low cytotoxicity. {ECO:0000250|UniProtKB:P9WID5}.
-!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
AMP from adenosine: step 1/1. {ECO:0000250|UniProtKB:P9WID5}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WID5}.
-!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
{ECO:0000305}.
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EMBL; AE000516; AAK46544.1; -; Genomic_DNA.
PIR; C70785; C70785.
RefSeq; WP_003411414.1; NZ_KK341227.1.
ProteinModelPortal; P9WID4; -.
SMR; P9WID4; -.
EnsemblBacteria; AAK46544; AAK46544; MT2258.
KEGG; mtc:MT2258; -.
PATRIC; fig|83331.31.peg.2433; -.
KO; K00856; -.
OrthoDB; POG091H08L7; -.
UniPathway; UPA00588; UER00659.
Proteomes; UP000001020; Chromosome.
GO; GO:0004001; F:adenosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
Gene3D; 3.40.1190.20; -; 1.
InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR029056; Ribokinase-like.
Pfam; PF00294; PfkB; 1.
SUPFAM; SSF53613; SSF53613; 1.
PROSITE; PS00583; PFKB_KINASES_1; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Kinase; Magnesium; Nucleotide-binding;
Purine salvage; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P9WID5}.
CHAIN 2 324 Adenosine kinase.
/FTId=PRO_0000428026.
NP_BIND 223 228 ATP. {ECO:0000250|UniProtKB:P9WID5}.
REGION 172 173 Substrate binding.
{ECO:0000250|UniProtKB:P9WID5}.
ACT_SITE 257 257 Proton acceptor.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 8 8 Substrate.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 12 12 Substrate.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 36 36 Substrate; shared with dimeric partner.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 48 48 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 52 52 Substrate.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 102 102 Substrate.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 116 116 Substrate.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 195 195 ATP. {ECO:0000250|UniProtKB:P9WID5}.
BINDING 256 256 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:P9WID5}.
BINDING 257 257 Substrate.
{ECO:0000250|UniProtKB:P9WID5}.
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


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