AIRSK_SALTY
ID AIRSK_SALTY Reviewed; 319 AA.
AC Q8ZKR2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Aminoimidazole riboside kinase {ECO:0000303|PubMed:15458630};
DE Short=AIRs kinase {ECO:0000303|PubMed:12486071};
DE EC=2.7.1.223 {ECO:0000269|PubMed:12486071};
GN OrderedLocusNames=STM4066 {ECO:0000312|EMBL:AAL22906.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=12486071; DOI=10.1128/jb.185.1.332-339.2003;
RA Dougherty M., Downs D.M.;
RT "The stm4066 gene product of Salmonella enterica serovar Typhimurium has
RT aminoimidazole riboside (AIRs) kinase activity and allows AIRs to satisfy
RT the thiamine requirement of pur mutant strains.";
RL J. Bacteriol. 185:332-339(2003).
RN [3] {ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP AMINOIMIDAZOLE RIBOSIDE; ATP ANALOG AND POTASSIUM IONS, ACTIVITY
RP REGULATION, SUBUNIT, DOMAIN, AND ACTIVE SITE.
RX PubMed=15458630; DOI=10.1016/j.str.2004.07.020;
RA Zhang Y., Dougherty M., Downs D.M., Ealick S.E.;
RT "Crystal structure of an aminoimidazole riboside kinase from Salmonella
RT enterica: implications for the evolution of the ribokinase superfamily.";
RL Structure 12:1809-1821(2004).
CC -!- FUNCTION: Phosphorylates 5-amino-1-(beta-D-ribosyl)imidazole (AIRs) to
CC form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important
CC intermediate in the purine and thiamine biosynthetic pathways
CC (PubMed:12486071). It allows the use of exogenous aminoimidazole
CC riboside (AIRs) to satisfy the cellular requirement for purines and
CC thiamine (PubMed:12486071). {ECO:0000269|PubMed:12486071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(beta-D-ribosyl)imidazole + ATP = 5-amino-1-(5-
CC phospho-beta-D-ribosyl)imidazole + ADP + H(+); Xref=Rhea:RHEA:44748,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:142407, ChEBI:CHEBI:456216; EC=2.7.1.223;
CC Evidence={ECO:0000269|PubMed:12486071};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44749;
CC Evidence={ECO:0000269|PubMed:12486071};
CC -!- ACTIVITY REGULATION: Potassium may regulate kinase activity.
CC {ECO:0000305|PubMed:15458630}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15458630}.
CC -!- INDUCTION: Repressed by STM4068. {ECO:0000269|PubMed:12486071}.
CC -!- DOMAIN: Does not show significant conformational changes upon substrate
CC binding. {ECO:0000269|PubMed:15458630}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene prevents the efficient use
CC of AIRs as a source of thiamine. {ECO:0000269|PubMed:12486071}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL22906.1; -; Genomic_DNA.
DR RefSeq; NP_462947.1; NC_003197.2.
DR RefSeq; WP_000646499.1; NC_003197.2.
DR PDB; 1TYY; X-ray; 2.60 A; A/B=1-319.
DR PDB; 1TZ3; X-ray; 2.90 A; A/B=1-319.
DR PDB; 1TZ6; X-ray; 2.70 A; A/B=1-319.
DR PDBsum; 1TYY; -.
DR PDBsum; 1TZ3; -.
DR PDBsum; 1TZ6; -.
DR AlphaFoldDB; Q8ZKR2; -.
DR SMR; Q8ZKR2; -.
DR STRING; 99287.STM4066; -.
DR DrugBank; DB04568; 5-Aminoimidazole Ribonucleoside.
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR PaxDb; Q8ZKR2; -.
DR EnsemblBacteria; AAL22906; AAL22906; STM4066.
DR GeneID; 1255593; -.
DR KEGG; stm:STM4066; -.
DR PATRIC; fig|99287.12.peg.4286; -.
DR HOGENOM; CLU_027634_6_1_6; -.
DR OMA; NWRPTFW; -.
DR PhylomeDB; Q8ZKR2; -.
DR BioCyc; MetaCyc:STM4066-MON; -.
DR BioCyc; SENT99287:STM4066-MON; -.
DR BRENDA; 2.7.1.223; 5542.
DR EvolutionaryTrace; Q8ZKR2; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; 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; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Metal-binding; Nucleotide-binding;
KW Potassium; Reference proteome; Transferase.
FT CHAIN 1..319
FT /note="Aminoimidazole riboside kinase"
FT /id="PRO_0000452103"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3"
FT BINDING 16
FT /ligand="5-amino-1-(beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:142407"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6"
FT BINDING 31
FT /ligand="5-amino-1-(beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:142407"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6"
FT BINDING 101
FT /ligand="5-amino-1-(beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:142407"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 158..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15458630,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 162
FT /ligand="5-amino-1-(beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:142407"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15458630,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15458630,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 213
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 220..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15458630,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 248
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 252
FT /ligand="5-amino-1-(beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:142407"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15458630,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 287
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3,
FT ECO:0007744|PDB:1TZ6"
FT BINDING 290
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6"
FT BINDING 292
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15458630,
FT ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:1TYY"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1TZ6"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1TYY"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:1TZ6"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 270..286
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1TYY"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1TYY"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:1TYY"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:1TYY"
SQ SEQUENCE 319 AA; 34238 MW; A899A6735BC25D66 CRC64;
MKAMNKVWVI GDASVDLVPE KQNSYLKCPG GASANVGVCV ARLGGECGFI GCLGDDDAGR
FLRQVFQDNG VDVTFLRLDA DLTSAVLIVN LTADGERSFT YLVHPGADTY VSPQDLPPFR
QYEWFYFSSI GLTDRPAREA CLEGARRMRE AGGYVLFDVN LRSKMWGNTD EIPELIARSA
ALASICKVSA DELCQLSGAS HWQDARYYLR DLGCDTTIIS LGADGALLIT AEGEFHFPAP
RVDVVDTTGA GDAFVGGLLF TLSRANCWDH ALLAEAISNA NACGAMAVTA KGAMTALPFP
DQLNTFLSSH SLAQAMTVK
