ID A0A0F5F0Z2_AVIPA Unreviewed; 267 AA.
AC A0A0F5F0Z2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ECO:0000313|EMBL:SUU96953.1};
GN ORFNames=HBL79_02985 {ECO:0000313|EMBL:QIR11298.1}, NCTC10926_00308
GN {ECO:0000313|EMBL:SUU96953.1}, OY678_06880
GN {ECO:0000313|EMBL:WAL55741.1};
OS Avibacterium paragallinarum (Haemophilus gallinarum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=728 {ECO:0000313|EMBL:SUU96953.1, ECO:0000313|Proteomes:UP000254620};
RN [1] {ECO:0000313|EMBL:SUU96953.1, ECO:0000313|Proteomes:UP000254620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10926 {ECO:0000313|EMBL:SUU96953.1,
RC ECO:0000313|Proteomes:UP000254620};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIR11298.1, ECO:0000313|Proteomes:UP000503595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESV-135 {ECO:0000313|EMBL:QIR11298.1,
RC ECO:0000313|Proteomes:UP000503595};
RA Cobos-Justo M.E., Sanchez-Alonso M.P., Negrete-Abascal E., Perez V.,
RA Soriano-Vargas E., Castelan H., Vazquez-Cruz C.;
RT "Comparison of the genome sequence of three Mexican strains of Avibacterium
RT paragallinarum.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:WAL55741.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-AP1 {ECO:0000313|EMBL:WAL55741.1};
RA Zhang J.P.;
RT "The genome of Avibacterium paragallinarum.";
RL Submitted (NOV-2022) 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}.
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DR EMBL; CP050316; QIR11298.1; -; Genomic_DNA.
DR EMBL; UFSW01000001; SUU96953.1; -; Genomic_DNA.
DR EMBL; CP113786; WAL55741.1; -; Genomic_DNA.
DR RefSeq; WP_035685744.1; NZ_VXDA01000038.1.
DR STRING; 728.VY92_08280; -.
DR GeneID; 66255552; -.
DR KEGG; apag:EIA51_06940; -.
DR eggNOG; COG2145; Bacteria.
DR OrthoDB; 8909021at2; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000254620; Unassembled WGS sequence.
DR Proteomes; UP000503595; Chromosome.
DR Proteomes; UP001163112; Chromosome.
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 NCBIfam; TIGR00694; thiM; 1.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
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:SUU96953.1};
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:SUU96953.1}.
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ SEQUENCE 267 AA; 27914 MW; 33EE73D9D8681662 CRC64;
MDFNLIAKIR KQNPLIHNIT NIVVANYVAN GLLALGASPI MADAEEEMAD LAKFSSVLVI
NIGTLDSYKV KAMLAAGKAA NQAGIPVVLD PVGVGATAYR KAVVAQLLSH IKFTAIRGNA
GEIAQLAGIH WSAKGVDAGQ GESDVAEIAK VAAQQYQCVV AVSGEVDYLS DGKQLATIHN
GTAMFPKITG SGCLLGAVIG AFLAVQPDQP FNATVQACTA YAVAGELAAE PLGAKKYGQF
YTALLDQLGE LEDQQVAQYA KVYYTDI
//
