THIM_CUTAK
ID THIM_CUTAK Reviewed; 277 AA.
AC Q6A9C5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE EC=2.7.1.50 {ECO:0000255|HAMAP-Rule:MF_00228};
DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE Short=TH kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE Short=Thz kinase {ECO:0000255|HAMAP-Rule:MF_00228};
GN Name=thiM {ECO:0000255|HAMAP-Rule:MF_00228}; OrderedLocusNames=PPA0885;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00228};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00228}.
CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00228}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT82641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017283; AAT82641.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002531443.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A9C5; -.
DR SMR; Q6A9C5; -.
DR STRING; 267747.PPA0885; -.
DR EnsemblBacteria; AAT82641; AAT82641; PPA0885.
DR KEGG; pac:PPA0885; -.
DR PATRIC; fig|267747.3.peg.918; -.
DR eggNOG; COG2145; Bacteria.
DR HOGENOM; CLU_019943_0_1_11; -.
DR OMA; KRPLVHN; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000000603; 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; SSF53613; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..277
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000383887"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ SEQUENCE 277 AA; 28469 MW; 12CECB33C6E876AD CRC64;
MPAKGVVDMT ELSNLVAESL ERLRRDKPLV QCLTNIVVAN FTANVLLSAG AVPAMVDNPE
ESEGFASIAD GVLVNTGTPY RETTEAMIAA ARGAASSNTP WVLDPVGVGM SWRTRVVLDT
LDVAAPAVIR ANASEVLALA GTGASSRGPE AGDAVEDALA SATQLVRHYG CVVAISGPVD
HILDADRHVT VSSGHEWMTR VTGVGCSLGA LTAAFAGIQN DHLIAAVSAT AMLCVVAERA
AERSAGPGAF AQALVDELFL VSPDEVGERG GLRDVTA
