THIL_PYRCJ
ID THIL_PYRCJ Reviewed; 293 AA.
AC A3MTW6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE Short=TMP kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE Short=TP kinase {ECO:0000303|PubMed:26639844};
DE Short=Thiamine-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000303|PubMed:26639844};
DE EC=2.7.4.16 {ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000269|PubMed:26639844};
GN Name=thiL {ECO:0000303|PubMed:26639844};
GN OrderedLocusNames=Pcal_0657 {ECO:0000312|EMBL:ABO08083.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, PATHWAY, SUBUNIT, AND MUTAGENESIS OF ARG-136 AND SER-196.
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RX PubMed=26639844; DOI=10.3177/jnsv.61.369;
RA Hayashi M., Nosaka K.;
RT "Characterization of thiamin phosphate kinase in the hyperthermophilic
RT archaeon Pyrobaculum calidifontis.";
RL J. Nutr. Sci. Vitaminol. 61:369-374(2015).
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 ECO:0000269|PubMed:26639844}.
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 ECO:0000269|PubMed:26639844};
CC -!- ACTIVITY REGULATION: Is inhibited by AMP; the mode of AMP inhibition is
CC uncompetitive for both TMP and ATP. {ECO:0000269|PubMed:26639844}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 uM for thiamine phosphate (at pH 7.0 and 100 degrees Celsius)
CC {ECO:0000269|PubMed:26639844};
CC KM=39 uM for ATP (at pH 7.0 and 100 degrees Celsius)
CC {ECO:0000269|PubMed:26639844};
CC Note=kcat is 0.063 sec(-1) (at pH 7.0 and 100 degrees Celsius).
CC {ECO:0000269|PubMed:26639844};
CC pH dependence:
CC Optimum pH is around 7.0. Retains about 90% of maximum activity at pH
CC 8.0. {ECO:0000269|PubMed:26639844};
CC Temperature dependence:
CC Optimum temperature is 120 degrees Celsius. Activities at 100 and 80
CC degrees Celsius are about 50% and 10% of that at 120 degrees Celsius,
CC respectively. Is unstable so that the protein loses about 45% of its
CC activity after heating for 15 minutes at 100 degrees Celsius.
CC However, the enzyme is not so intensively inactivated in the presence
CC of ATP. {ECO:0000269|PubMed:26639844};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine phosphate: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000269|PubMed:26639844}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26639844}.
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; CP000561; ABO08083.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MTW6; -.
DR SMR; A3MTW6; -.
DR STRING; 410359.Pcal_0657; -.
DR EnsemblBacteria; ABO08083; ABO08083; Pcal_0657.
DR KEGG; pcl:Pcal_0657; -.
DR eggNOG; arCOG00638; Archaea.
DR HOGENOM; CLU_046964_2_1_2; -.
DR OMA; DFGWRNV; -.
DR BRENDA; 2.7.4.16; 7282.
DR UniPathway; UPA00060; UER00142.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; 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 SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..293
FT /note="Thiamine-monophosphate kinase"
FT /id="PRO_0000439888"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 112..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02128"
FT MUTAGEN 136
FT /note="R->M: 7-fold decrease in affinity for ATP. 1.5-fold
FT increase in activity."
FT /evidence="ECO:0000269|PubMed:26639844"
FT MUTAGEN 196
FT /note="S->A: 90% decrease in activity. However, displays a
FT 30-fold increase in the catalytic efficiency toward ATP due
FT to a large increase in affinity for ATP."
FT /evidence="ECO:0000269|PubMed:26639844"
SQ SEQUENCE 293 AA; 32000 MW; 62778CDB7900822F CRC64;
MSGFGGRGVD EKGFLRWLLG ELGVEEDDVA YVDGLVVKVD GAAASTSRLP FQTWADFGWR
NVAAAYSDVR VKFAEARLLL ASVTAPDLGT AAEVVQGVRE ASQFFSLAYV GGDLNEGRDV
VVDVVLVGWA RARVGRAPRP GDVLVTIPQF GYTSLAYRFW QMGGAVVERG VEALKRPKPL
WPLPPAECVT AAMDSSDGLG DVLWSMARGV DIVVKELPAP REVLEFAAER GLDVGEIVFN
GGEEFLPVFA VRRDCPVESP YVSFAEVVPG EGRVWWRGEE LKWRGWAYFR GWG
