GenomeNet

Database: UniProt
Entry: A0A0W0TWB0_9GAMM
LinkDB: A0A0W0TWB0_9GAMM
Original site: A0A0W0TWB0_9GAMM 
ID   A0A0W0TWB0_9GAMM        Unreviewed;       322 AA.
AC   A0A0W0TWB0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:KTC99702.1};
GN   ORFNames=E4T54_10730 {ECO:0000313|EMBL:QBS13175.1}, Lgee_1194
GN   {ECO:0000313|EMBL:KTC99702.1};
OS   Legionella geestiana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45065 {ECO:0000313|EMBL:KTC99702.1, ECO:0000313|Proteomes:UP000054785};
RN   [1] {ECO:0000313|EMBL:KTC99702.1, ECO:0000313|Proteomes:UP000054785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTC99702.1,
RC   ECO:0000313|Proteomes:UP000054785};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QBS13175.1, ECO:0000313|Proteomes:UP000294523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1308 {ECO:0000313|EMBL:QBS13175.1,
RC   ECO:0000313|Proteomes:UP000294523};
RA   Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA   Charpentier X.;
RT   "Diverse conjugative elements silence natural transformation in Legionella
RT   species.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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=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: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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02128}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNYC01000044; KTC99702.1; -; Genomic_DNA.
DR   EMBL; CP038271; QBS13175.1; -; Genomic_DNA.
DR   RefSeq; WP_028386303.1; NZ_UGNZ01000001.1.
DR   AlphaFoldDB; A0A0W0TWB0; -.
DR   STRING; 45065.Lgee_1194; -.
DR   KEGG; lgt:E4T54_10730; -.
DR   PATRIC; fig|45065.4.peg.1285; -.
DR   OrthoDB; 9802811at2; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000054785; Unassembled WGS sequence.
DR   Proteomes; UP000294523; 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; 3.90.650.10; 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; 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-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   Pfam; PF02769; AIRS_C; 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:KTC99702.1};
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:UP000054785};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:KTC99702.1}.
FT   DOMAIN          27..137
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          150..301
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         120..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
SQ   SEQUENCE   322 AA;  34181 MW;  564B0D13178294C4 CRC64;
     MDEFALIETF FKRPFAATDS ELILGIGDDG ALLKVPPDME LVVCTDTLVE GVHFPPGLDA
     GMLAERAVRV NVSDLAAMGA TPRWASLALT LPALSENWMK TFSQGLCNAL TRYGMTLIGG
     DTTRGPLCIT LTVQGLVPSG RALRRSGAAS GNVIVVTGML GAAALAVECL HGLQVPENDR
     ETLMQALLLP EPRVDVAGVL RDFATAAIDV SDGLGADLQH LCRASGVGAC LMMQKLPVHP
     LVQKYASERA MTLALEGGDD YVLCFTVPPA HLEACRDALS QCGVTCYPVG YIEDGAHMRL
     TDATGTNHPF TPRGYNHFQE TA
//
DBGET integrated database retrieval system