THIK_SALA4
ID THIK_SALA4 Reviewed; 274 AA.
AC B5F8E6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Thiamine kinase {ECO:0000255|HAMAP-Rule:MF_01604};
DE EC=2.7.1.89 {ECO:0000255|HAMAP-Rule:MF_01604};
GN Name=thiK {ECO:0000255|HAMAP-Rule:MF_01604}; OrderedLocusNames=SeAg_B1977;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_01604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine = ADP + H(+) + thiamine phosphate;
CC Xref=Rhea:RHEA:12012, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, ChEBI:CHEBI:456216;
CC EC=2.7.1.89; Evidence={ECO:0000255|HAMAP-Rule:MF_01604};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from thiamine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01604}.
CC -!- SIMILARITY: Belongs to the thiamine kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_01604}.
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DR EMBL; CP001138; ACH51479.1; -; Genomic_DNA.
DR RefSeq; WP_001257320.1; NC_011149.1.
DR AlphaFoldDB; B5F8E6; -.
DR SMR; B5F8E6; -.
DR EnsemblBacteria; ACH51479; ACH51479; SeAg_B1977.
DR KEGG; sea:SeAg_B1977; -.
DR HOGENOM; CLU_055115_2_1_6; -.
DR OMA; DVHAGNI; -.
DR UniPathway; UPA00060; UER00596.
DR Proteomes; UP000008819; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019165; F:thiamine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR HAMAP; MF_01604; Thiamine_kinase; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014093; Thiamine_kinase.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR02721; ycfN_thiK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..274
FT /note="Thiamine kinase"
FT /id="PRO_1000198094"
SQ SEQUENCE 274 AA; 31899 MW; 2651075A6A747B03 CRC64;
MRSNNNNPLT RDEILSRYFP QYRPAVAASQ GLSGGSCIIA HDTHRIVLRR HHDPDAPPAH
FLRHHRALSQ LPASLAPRAL FYTPGWMAVE YLHGVVNSAL PDADELAALL YHLHQQPRFG
WRIALSPLLA QYWSCCDPAR RTPFWLRRLK QLQKNGEPRP LRLAPLHMDV HGDNIVLTSA
GLRLIDWEYA GDGDIALELA AVWVEDERQH RQLADAYAAR ARIDARQLWR QIRLWHPWVI
MLKAGWFEYR WRQTGEQQFI RLADETWRQL RMKG