ID I4BY82_ACEMN Unreviewed; 270 AA.
AC I4BY82;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 OrderedLocusNames=Anamo_1644 {ECO:0000313|EMBL:AFM22239.1};
OS Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / JCM 12221 / NGA)
OS (Anaerobaculum mobile).
OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC Acetomicrobium.
OX NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM22239.1, ECO:0000313|Proteomes:UP000006061};
RN [1] {ECO:0000313|Proteomes:UP000006061}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-54 / DSM 13181 / NGA
RC {ECO:0000313|Proteomes:UP000006061};
RX PubMed=23961311; DOI=10.4056/sigs.3547050;
RA Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Spring S., Goker M., Woyke T.,
RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the moderate thermophile Anaerobaculum mobile
RT type strain (NGA(T)).";
RL Stand. Genomic Sci. 8:47-57(2013).
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; CP003198; AFM22239.1; -; Genomic_DNA.
DR RefSeq; WP_014807463.1; NC_018024.1.
DR AlphaFoldDB; I4BY82; -.
DR STRING; 891968.Anamo_1644; -.
DR KEGG; amo:Anamo_1644; -.
DR PATRIC; fig|891968.3.peg.1638; -.
DR eggNOG; COG2145; Bacteria.
DR HOGENOM; CLU_019943_0_1_0; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000006061; 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 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:AFM22239.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000006061};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00228}; Transferase {ECO:0000256|HAMAP-Rule:MF_00228}.
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ SEQUENCE 270 AA; 29035 MW; 4D0229A103AA2A78 CRC64;
MFDLKRVDFS KVLKDVTLRK PLIYHMTNGV AMSEQAHLAL AIGASPVMSL YPGEAAELIS
VADVLLVNIG TPSREGIEAM FVAVREAREL GKPAILDPVG YGATKMRVDL VNRLLDTKAF
RVIKGNGAEI SLLGGQEAQV RGVDSMDSPR TALAVKTLAL KHDCIAVATG PTDYVSDGKD
VYALRRGHEW LTLLSGSGCY VGTMMAAYMS VTEPLIAAMT ALALMSVASE VAAMKSDGPG
TFRANLFDIL HDFSLNPSSF DMPIWEKLEI
//
