ID A0A0G3CJ48_9GAMM Unreviewed; 283 AA.
AC A0A0G3CJ48;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Thiamine kinase {ECO:0000256|HAMAP-Rule:MF_01604};
DE EC=2.7.1.89 {ECO:0000256|HAMAP-Rule:MF_01604};
GN Name=thiK {ECO:0000256|HAMAP-Rule:MF_01604};
GN ORFNames=QQ39_07990 {ECO:0000313|EMBL:AKJ42031.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ42031.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ42031.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ42031.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(2015).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC phosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01604};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from thiamine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01604}.
CC -!- SIMILARITY: Belongs to the thiamine kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_01604}.
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DR EMBL; CP010423; AKJ42031.1; -; Genomic_DNA.
DR RefSeq; WP_047780770.1; NZ_CP010423.1.
DR AlphaFoldDB; A0A0G3CJ48; -.
DR STRING; 82985.QQ39_07990; -.
DR KEGG; pfq:QQ39_07990; -.
DR OrthoDB; 179763at2; -.
DR UniPathway; UPA00060; UER00596.
DR Proteomes; UP000068021; 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 Gene3D; 3.90.1200.10; -; 1.
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; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01604};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01604};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01604};
KW Reference proteome {ECO:0000313|Proteomes:UP000068021};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01604}.
FT DOMAIN 66..238
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 283 AA; 32684 MW; 72A7CBF30D332B1F CRC64;
MFSVNSQLTQ LISRHLPGYS AEELSINPVS GLTGTSWQIA NHHPCWLAKP LARTDAVLGI
NRWREYNFLK RLSAVGLAAA PLLITNQWLI SGWIDGQLMD KATWISADGR SMLADSLVKL
HRQPTVGFSL DLHQRFIRYW QSIDRHRITP NWLRLHQSML RSPCPRPLKL APTHLDLHPD
NIVLTVNGPV LIDWEYAIDA DIAFELAALF DGNRWDQAAE TDFLQHYIRA GGYEDLETLA
RQVALWKPYT HYLMLMWYET RWQQTRNPLY LEASDLLRSD YAI
//
