ADOK_MYCBO
ID ADOK_MYCBO Reviewed; 324 AA.
AC P83736; A0A1R3Y0H7; Q10391; X2BK30;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Adenosine kinase {ECO:0000303|Ref.3};
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=BQ2027_MB2225C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH 2-FLUOROADENOSINE.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RA Reddy M.C.M., Palaninathan S.K., Shetty N.D., Owen J.L., Watson M.D.,
RA Sacchettini J.C.;
RT "Crystal structure of M.tuberculosis adenosine kinase complexed with 2-
RT fluoro-adenosine.";
RL Submitted (AUG-2014) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of adenosine to adenosine
CC monophosphate (AMP). Prefers dGTP and GTP to ATP as phosphate donors in
CC 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 -!- 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; LT708304; SIU00833.1; -; Genomic_DNA.
DR RefSeq; NP_855874.1; NC_002945.3.
DR RefSeq; WP_003411414.1; NC_002945.4.
DR PDB; 4UBE; X-ray; 1.93 A; A=1-324.
DR PDBsum; 4UBE; -.
DR AlphaFoldDB; P83736; -.
DR SMR; P83736; -.
DR EnsemblBacteria; SIU00833; SIU00833; BQ2027_MB2225C.
DR GeneID; 45426178; -.
DR PATRIC; fig|233413.5.peg.2441; -.
DR OMA; SQQIARM; -.
DR UniPathway; UPA00588; UER00659.
DR Proteomes; UP000001419; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Nucleotide-binding;
KW Purine salvage; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..324
FT /note="Adenosine kinase"
FT /id="PRO_0000080063"
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:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 12
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 36
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 48
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 52
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 102
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 116
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT BINDING 172..173
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4UBE"
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:0000305|Ref.3, ECO:0007744|PDB:4UBE"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:4UBE"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4UBE"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:4UBE"
FT TURN 184..188
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 273..288
FT /evidence="ECO:0007829|PDB:4UBE"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:4UBE"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:4UBE"
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
