THIL_BUCAP
ID THIL_BUCAP Reviewed; 323 AA.
AC Q8K9A5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE Short=TMP kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE Short=Thiamine-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE EC=2.7.4.16 {ECO:0000255|HAMAP-Rule:MF_02128};
GN Name=thiL {ECO:0000255|HAMAP-Rule:MF_02128}; OrderedLocusNames=BUsg_444;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-
CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active
CC form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate;
CC Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02128};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine phosphate: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02128}.
CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a direct,
CC inline transfer of the gamma-phosphate of ATP to TMP rather than a
CC phosphorylated enzyme intermediate. {ECO:0000255|HAMAP-Rule:MF_02128}.
CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_02128}.
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DR EMBL; AE013218; AAM67987.1; -; Genomic_DNA.
DR RefSeq; WP_011053954.1; NC_004061.1.
DR AlphaFoldDB; Q8K9A5; -.
DR SMR; Q8K9A5; -.
DR STRING; 198804.BUsg_444; -.
DR EnsemblBacteria; AAM67987; AAM67987; BUsg_444.
DR KEGG; bas:BUsg_444; -.
DR eggNOG; COG0611; Bacteria.
DR HOGENOM; CLU_046964_3_0_6; -.
DR OMA; HFRRDWS; -.
DR OrthoDB; 1016556at2; -.
DR UniPathway; UPA00060; UER00142.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02194; ThiL; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_02128; TMP_kinase; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR006283; ThiL.
DR PANTHER; PTHR30270; PTHR30270; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR01379; thiL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..323
FT /note="Thiamine-monophosphate kinase"
FT /id="PRO_0000096193"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 121..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
SQ SEQUENCE 323 AA; 35838 MW; DF6512D5D6DD9CDF CRC64;
MEYNEFEIIS KFFKNHQKKD KNQIKGIGDD SALIKIPKNN LLAISTDTLV EGKHFLKNIT
PKDLAYKSVA VNLSDLAAMG AKPTWITLSI TMPKSDSVWL KSFSKSFFKI LNKYKLNLIG
GDTNSGPLSI TLSIYGLIEG KNALLRGNAK NGDLIYITGN LGESAAGLSL LQKKTFLKNV
KICNYLIKKH LKPIPRISEG IALRNIANAA IDISDGLISD LGHILKNSKC GADINLNTIP
ISKILTDNFK IDEYLNWALN SGEDYELCFT ISKKNIKKLN VAIKKKIIKC TCIGYITSAE
KGLNLIQNQK KIIFKKSGFN HFI
