ID A0A120A101_BACSE Unreviewed; 353 AA.
AC A0A120A101;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE Short=TMP kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE Short=Thiamine-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE EC=2.7.4.16 {ECO:0000256|HAMAP-Rule:MF_02128};
GN Name=thiL {ECO:0000256|HAMAP-Rule:MF_02128,
GN ECO:0000313|EMBL:KWR52854.1};
GN ORFNames=AA415_02720 {ECO:0000313|EMBL:KWR52854.1}, DW668_05335
GN {ECO:0000313|EMBL:RHF76744.1}, DW889_16380
GN {ECO:0000313|EMBL:RHB23035.1}, DWY58_17520
GN {ECO:0000313|EMBL:RGR25830.1}, DXC34_17675
GN {ECO:0000313|EMBL:RGM09274.1}, F9950_15570
GN {ECO:0000313|EMBL:KAB5324910.1}, F9958_14825
GN {ECO:0000313|EMBL:KAB5310992.1}, F9962_14725
GN {ECO:0000313|EMBL:KAB5279785.1};
OS Bacteroides stercoris.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Bacteroidaceae; Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR52854.1, ECO:0000313|Proteomes:UP000056419};
RN [1] {ECO:0000313|EMBL:KWR52854.1, ECO:0000313|Proteomes:UP000056419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR52854.1,
RC ECO:0000313|Proteomes:UP000056419};
RX PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA Coyne M.J., Roelofs K.G., Comstock L.E.;
RT "Type VI secretion systems of human gut Bacteroidales segregate into three
RT genetic architectures, two of which are contained on mobile genetic
RT elements.";
RL BMC Genomics 17:58-58(2016).
RN [2] {ECO:0000313|EMBL:KWR52854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR52854.1};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000261223, ECO:0000313|Proteomes:UP000283482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF25-6 {ECO:0000313|EMBL:RGR25830.1,
RC ECO:0000313|Proteomes:UP000284161}, AM25-16
RC {ECO:0000313|EMBL:RHF76744.1, ECO:0000313|Proteomes:UP000283762},
RC AM40-34 {ECO:0000313|EMBL:RHB23035.1,
RC ECO:0000313|Proteomes:UP000283482}, and TF03-6
RC {ECO:0000313|EMBL:RGM09274.1, ECO:0000313|Proteomes:UP000261223};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000431177, ECO:0000313|Proteomes:UP000440773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A17 {ECO:0000313|EMBL:KAB5279785.1,
RC ECO:0000313|Proteomes:UP000440773}, BIOML-A2
RC {ECO:0000313|EMBL:KAB5324910.1, ECO:0000313|Proteomes:UP000431177},
RC and BIOML-A6 {ECO:0000313|EMBL:KAB5310992.1,
RC ECO:0000313|Proteomes:UP000467334};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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:0000256|HAMAP-Rule:MF_02128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiamine phosphate + ATP = thiamine diphosphate + ADP;
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:0000256|HAMAP-Rule:MF_02128};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine phosphate: step 1/1.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_02128}.
CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_02128}.
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:KWR52854.1}.
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DR EMBL; WCLP01000044; KAB5279785.1; -; Genomic_DNA.
DR EMBL; WCLE01000041; KAB5310992.1; -; Genomic_DNA.
DR EMBL; WCLA01000042; KAB5324910.1; -; Genomic_DNA.
DR EMBL; LRGC01000017; KWR52854.1; -; Genomic_DNA.
DR EMBL; QSSV01000036; RGM09274.1; -; Genomic_DNA.
DR EMBL; QRUB01000033; RGR25830.1; -; Genomic_DNA.
DR EMBL; QSGN01000067; RHB23035.1; -; Genomic_DNA.
DR EMBL; QRHJ01000010; RHF76744.1; -; Genomic_DNA.
DR RefSeq; WP_005656857.1; NZ_CAXVLE010000029.1.
DR AlphaFoldDB; A0A120A101; -.
DR STRING; 46506.AA415_02720; -.
DR GeneID; 31798145; -.
DR PATRIC; fig|46506.5.peg.2921; -.
DR UniPathway; UPA00060; UER00142.
DR Proteomes; UP000056419; Unassembled WGS sequence.
DR Proteomes; UP000261223; Unassembled WGS sequence.
DR Proteomes; UP000283482; Unassembled WGS sequence.
DR Proteomes; UP000283762; Unassembled WGS sequence.
DR Proteomes; UP000284161; Unassembled WGS sequence.
DR Proteomes; UP000431177; Unassembled WGS sequence.
DR Proteomes; UP000440773; Unassembled WGS sequence.
DR Proteomes; UP000467334; Unassembled WGS sequence.
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: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; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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-like.
DR NCBIfam; TIGR01379; thiL; 1.
DR PANTHER; PTHR30270; THIAMINE-MONOPHOSPHATE KINASE; 1.
DR PANTHER; PTHR30270:SF0; THIAMINE-MONOPHOSPHATE KINASE; 1.
DR Pfam; PF00586; AIRS; 1.
DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:KWR52854.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02128};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW Reference proteome {ECO:0000313|Proteomes:UP000056419};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_02128};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:KWR52854.1}.
FT DOMAIN 33..145
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 128..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
SQ SEQUENCE 353 AA; 38920 MW; 0C873976328D56AD CRC64;
MRTEIATLGE FGLIRHLTES IELKNESSRY GIGDDAAVLS YPADKEVLVT TDLLLEGVHF
DLTYVPLKHL GYKSAVVNFS DIYAMNGTPR QITVSLGLSK RFSVEDMEEL YAGIRLACEE
YGVDIVGGDT SSSYTGLTIS ITCIGEGEKG KVVYRNGAKE TDLICVSGDL GAAYMGLQLL
EREKSVLKGG DKDLQPDFAG KEYLLERQLK PEARRDIIQK LAKEGIQPTS MMDVSDGLSS
ELLHICTQSK VGCRIYEEHI PIDYQTAVMA EEFNMNLTTC ALNGGEDYEL LFTVPIADHE
KVSEMEGIKL IGHITKPELG CALISRDGQE FELKAQGWNP LKEESAAQQE EVE
//
