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Database: UniProt
Entry: Q87RU2_VIBPA
LinkDB: Q87RU2_VIBPA
Original site: Q87RU2_VIBPA 
ID   Q87RU2_VIBPA            Unreviewed;       321 AA.
AC   Q87RU2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 103.
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   OrderedLocusNames=VP0684 {ECO:0000313|EMBL:BAC58947.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC58947.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC58947.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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}.
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DR   EMBL; BA000031; BAC58947.1; -; Genomic_DNA.
DR   RefSeq; NP_797063.1; NC_004603.1.
DR   RefSeq; WP_005456036.1; NC_004603.1.
DR   AlphaFoldDB; Q87RU2; -.
DR   GeneID; 1188159; -.
DR   KEGG; vpa:VP0684; -.
DR   PATRIC; fig|223926.6.peg.652; -.
DR   eggNOG; COG0611; Bacteria.
DR   HOGENOM; CLU_046964_3_0_6; -.
DR   OMA; HFRRDWS; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000002493; Chromosome 1.
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:BAC58947.1};
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:UP000002493};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   DOMAIN          27..137
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          149..303
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         44
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         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
SQ   SEQUENCE   321 AA;  34532 MW;  FFF282C7B28BE54C CRC64;
     MSGEFNLIDK YFVGRQNQRK DVHLAAGDDC ALVKAPANVQ IAISTDTLVA GTHFLPHANP
     AWVAHKALAS NISDLAAMGA TPAWVSFALT MPEVDEEWLA PFCNAFFELA DYFGIQLIGG
     DTTKGPLSLT LTVQGFVPEG KALTRSGAKV GDWVYVTGNL GDAKAGLDVI LDETLRSRIG
     ADELEKAHYL STPRVLAGQA LVGLASSAID ISDGLISDIK HILKRSQVGV SIDVSQLPIS
     SELVQFLDDK VSAQQYALSS GEEYELCFTV SEQNRGSLQS ALSYSGCKVT CIGQIRPNGT
     FELHDNNQPL DWDLSGFDHF K
//
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