THIL_CAUVC
ID THIL_CAUVC Reviewed; 352 AA.
AC Q9A8J2;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=CC_1361;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK23342.1; -; Genomic_DNA.
DR PIR; B87418; B87418.
DR RefSeq; NP_420174.1; NC_002696.2.
DR RefSeq; WP_010919238.1; NC_002696.2.
DR AlphaFoldDB; Q9A8J2; -.
DR SMR; Q9A8J2; -.
DR STRING; 190650.CC_1361; -.
DR EnsemblBacteria; AAK23342; AAK23342; CC_1361.
DR KEGG; ccr:CC_1361; -.
DR PATRIC; fig|190650.5.peg.1391; -.
DR eggNOG; COG0611; Bacteria.
DR HOGENOM; CLU_046964_3_0_5; -.
DR OMA; HFRRDWS; -.
DR BioCyc; CAULO:CC1361-MON; -.
DR UniPathway; UPA00060; UER00142.
DR Proteomes; UP000001816; 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 Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..352
FT /note="Thiamine-monophosphate kinase"
FT /id="PRO_0000415635"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 150..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
SQ SEQUENCE 352 AA; 37486 MW; EF662C3F6D77F7DA CRC64;
MAPSTRSPVM HETDEEDWFA EDDAAAPAAA PPTEFDHIAR LLRPLTRGDP VALDLLDDAA
VLPSRPGYDL VITKDAMVAG VHFLAEEALD VVARKLLRTN LSDLAAKAAE PYGYFLAVGW
PSGSDVASRE TFARGLAEDG ALFDISLLGG DTVTTSGPLV VSATFLGWAP QGETILRRGA
KPGDRLMVSG TIGDGWLGLL AQWGEVMDAD GAMLRRYRQP EPRVTLRDAM RVHAKAAADV
SDGLLADSSH IAKASGCRVR VDLERLPLSP GAQAWLDQQP EQVEGRISLA SGGDDYEIVC
AVDPNEAWAF RVAAAAAGVK VSEIGEFVEG EGVSAYYKGR DVTPSRLGWL HG
