ID I8AFI6_9BACI Unreviewed; 328 AA.
AC I8AFI6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ORFNames=A374_15554 {ECO:0000313|EMBL:EIT84397.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT84397.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT84397.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT84397.1,
RC ECO:0000313|Proteomes:UP000004080};
RX PubMed=22887677; DOI=10.1128/JB.01049-12;
RA Cai L., Zhang T.;
RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL J. Bacteriol. 194:4780-4780(2012).
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 -!- 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:EIT84397.1}.
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DR EMBL; AKKV01000035; EIT84397.1; -; Genomic_DNA.
DR RefSeq; WP_007203184.1; NZ_AKKV01000035.1.
DR AlphaFoldDB; I8AFI6; -.
DR STRING; 1196324.A374_15554; -.
DR PATRIC; fig|1196324.3.peg.3186; -.
DR eggNOG; COG0611; Bacteria.
DR OrthoDB; 9802811at2; -.
DR UniPathway; UPA00060; UER00142.
DR Proteomes; UP000004080; 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: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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02128};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:EIT84397.1};
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:UP000004080};
KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:EIT84397.1}.
FT DOMAIN 26..140
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 152..303
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 52
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 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 121..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
SQ SEQUENCE 328 AA; 35359 MW; 53756132C91B6943 CRC64;
MRDEFAWIAS ITPKEHRQAS LLEGIGDDAA LVKGSEEEDQ VVCLDTMVEG VHFTTDTMAP
FHIGHKALAA NISDVAAMGG IPRYYLVSIA VPASWSEEAL GEIYKGMDTL AETYKMDLIG
GDTVSTKGPL VLSITVIGSV ESGKKLLRRN ARPGDVVFMT GCAGDAAGGL ALLLEHTRNH
PFTLTEQALV QAHQLPLPNV EAGRLLAEAN VRVALNDISD GVASEATEIA ESSGVKLTLV
WDKLPKSIAL QSYPQEQQEQ WLLYGGEDYT LIGTMAQEDF SLIQQKAKDC NLSFIAVGKV
EAGAPAVWLE RSQQPIEALH KAGYNHFS
//
