ID D1NSS7_9BIFI Unreviewed; 298 AA.
AC D1NSS7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Hydroxyethylthiazole kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE EC=2.7.1.50 {ECO:0000256|HAMAP-Rule:MF_00228};
DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE Short=TH kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE Short=Thz kinase {ECO:0000256|HAMAP-Rule:MF_00228};
GN Name=thiM {ECO:0000256|HAMAP-Rule:MF_00228};
GN ORFNames=BGLCM_0845 {ECO:0000313|EMBL:KFI59252.1}, BIFGAL_02837
GN {ECO:0000313|EMBL:EFA23729.1};
OS Bifidobacterium gallicum DSM 20093 = LMG 11596.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=561180 {ECO:0000313|EMBL:EFA23729.1, ECO:0000313|Proteomes:UP000003656};
RN [1] {ECO:0000313|EMBL:EFA23729.1, ECO:0000313|Proteomes:UP000003656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20093 {ECO:0000313|EMBL:EFA23729.1,
RC ECO:0000313|Proteomes:UP000003656};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFI59252.1, ECO:0000313|Proteomes:UP000029074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11596 {ECO:0000313|EMBL:KFI59252.1,
RC ECO:0000313|Proteomes:UP000029074};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000256|HAMAP-
CC Rule:MF_00228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-
CC phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50;
CC Evidence={ECO:0000256|ARBA:ARBA00001771, ECO:0000256|HAMAP-
CC Rule:MF_00228};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00228};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-
CC methylthiazole: step 1/1. {ECO:0000256|ARBA:ARBA00004868,
CC ECO:0000256|HAMAP-Rule:MF_00228}.
CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00228}.
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:EFA23729.1}.
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DR EMBL; ABXB03000001; EFA23729.1; -; Genomic_DNA.
DR EMBL; JGYW01000004; KFI59252.1; -; Genomic_DNA.
DR RefSeq; WP_006294244.1; NZ_JGYW01000004.1.
DR AlphaFoldDB; D1NSS7; -.
DR STRING; 561180.BIFGAL_02837; -.
DR eggNOG; COG2145; Bacteria.
DR OrthoDB; 8909021at2; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000003656; Unassembled WGS sequence.
DR Proteomes; UP000029074; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; 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-UniPathway.
DR CDD; cd01170; THZ_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00228; Thz_kinase; 1.
DR InterPro; IPR000417; Hyethyz_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF02110; HK; 1.
DR PIRSF; PIRSF000513; Thz_kinase; 1.
DR PRINTS; PR01099; HYETHTZKNASE.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:EFA23729.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00228};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:KFI59252.1}.
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ SEQUENCE 298 AA; 30626 MW; 03C44FD80E0EF823 CRC64;
MNMPAQDPIR LAIAEAVQQV HDTTPMAPSF TNFVTINLVA NAQLACGGSA AMSFLSNEFS
AVAALAKAAY INVGTLMPSY PDALRAITAD LKESGKPWVL DPVAAGLGAT RTNILMDMRH
NPPTIVRGNA SEIIALASMW GLIEGSSSNG PEGVESADDV QSAIEPARLL ARFLAQHSPD
GKAAVAVSGE TDLVTDGTRT FRLPGGSPLM TKITGAGCSL GGVTAVYLCV AEPLIAALAA
SALYNVAAEC AVRTLTSYTK VNPDTVALGP GTFQPAFLDA LAAATPEQVA SATLLEDK
//
