(data stored in ACNUC7421 zone)

SWISSPROT: THIM_EXIS2

ID   THIM_EXIS2              Reviewed;         256 AA.
AC   B1YJJ2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 74.
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=Exig_0541;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001022; ACB60022.1; -; Genomic_DNA.
DR   RefSeq; WP_012369446.1; NC_010556.1.
DR   SMR; B1YJJ2; -.
DR   STRING; 262543.Exig_0541; -.
DR   EnsemblBacteria; ACB60022; ACB60022; Exig_0541.
DR   KEGG; esi:Exig_0541; -.
DR   eggNOG; ENOG4105C4U; Bacteria.
DR   eggNOG; COG2145; LUCA.
DR   HOGENOM; HOG000114352; -.
DR   KO; K00878; -.
DR   OMA; KPIMAEH; -.
DR   OrthoDB; 1717689at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000001681; 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: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;
DR   PRODOM; B1YJJ2.
DR   SWISS-2DPAGE; B1YJJ2.
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..256
FT                   /note="Hydroxyethylthiazole kinase"
FT                   /id="PRO_0000383860"
FT   BINDING         37
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         113
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         159
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         186
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   256 AA;  27083 MW;  9718D1BC3D51DEE3 CRC64;
     MLRRIHDKKP LIHHLTNTVT INDCANMTLA LGGSPVMAED LLEVEEMVGL ADAVVINTGT
     INPDMRKAQL LAGKTANRLG KPVILDPVGA GATTLRTDFM KQLMEEITFT VIKGNASEIK
     TLLGQAARTK GVDVAEGESL DLQSVHAFAS QTKQVIVVTG PVDFVTDGVR QHHLDVGTKR
     LGQVTGTGCM TASLIATFLG AGYGRFDAAV FGTYAMGKAG ETAGNRPGIG SFRTGLFDAV
     SLMTEESLPE VQMNGQ
//

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