ID I0QVP5_9GAMM Unreviewed; 288 AA.
AC I0QVP5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=SPM24T3_05873 {ECO:0000313|EMBL:EIC85368.1};
OS Serratia sp. M24T3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC85368.1, ECO:0000313|Proteomes:UP000011072};
RN [1] {ECO:0000313|EMBL:EIC85368.1, ECO:0000313|Proteomes:UP000011072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC85368.1,
RC ECO:0000313|Proteomes:UP000011072};
RX PubMed=22740681; DOI=10.1128/JB.00670-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT Disease Nematode Bursaphelenchus xylophilus.";
RL J. Bacteriol. 194:3764-3764(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIC85368.1}.
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DR EMBL; AJHJ01000005; EIC85368.1; -; Genomic_DNA.
DR AlphaFoldDB; I0QVP5; -.
DR STRING; 932213.SPM24T3_05873; -.
DR PATRIC; fig|932213.3.peg.1179; -.
DR eggNOG; COG0510; Bacteria.
DR UniPathway; UPA00060; UER00596.
DR Proteomes; UP000011072; Unassembled WGS sequence.
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 PANTHER; PTHR40086:SF1; CELL CYCLE REGULATOR CCRZ; 1.
DR PANTHER; PTHR40086; PHOSPHOTRANSFERASE YTMP-RELATED; 1.
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, ECO:0000313|EMBL:EIC85368.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01604};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01604}.
FT DOMAIN 33..237
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 288 AA; 34005 MW; 956D69B4DD37AECF CRC64;
MQFKIRINPL LETWVEKYLP ADYSAGCIFT PVEGLSSESW RIEAASGVYL ARLQSTEKRQ
LGIDRRRENR LLRHLSSKHI APQVYAWACP WLVVNWIAGE TLDDKHFFAA QPQQQLAALL
AKLHRSQPCG ETLDIKKRFA DYWQLIDRRR LTPSWLHLHK RLLKQRLPRA LKISLAHMDI
HPQNWVNSPE GIRLIDWEYA VSADIGLEFA ALFSGNAYSK TQRYELLQQY ARQGGYGDAA
KLERQVRQWR LWLEYLMLMW FEVRWQQTAD IRYASWAQPL RQKLLSEF
//
