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Database: UniProt
Entry: THI4_THEKO
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ID   THI4_THEKO              Reviewed;         251 AA.
AC   Q5JD25;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-JUL-2019, entry version 92.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00304};
DE            EC=2.4.2.59 {ECO:0000255|HAMAP-Rule:MF_00304};
GN   Name=thi4 {ECO:0000255|HAMAP-Rule:MF_00304}; OrderedLocusNames=TK0434;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   LACK OF RIBOSE BISPHOSPHATE ISOMERASE ACTIVITY.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=17303759; DOI=10.1126/science.1135999;
RA   Sato T., Atomi H., Imanaka T.;
RT   "Archaeal type III RuBisCOs function in a pathway for AMP
RT   metabolism.";
RL   Science 315:1003-1006(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of the thiazole moiety of
CC       thiamine. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate
CC       (ADT), an adenylated thiazole intermediate, using free sulfide as
CC       a source of sulfur. {ECO:0000255|HAMAP-Rule:MF_00304}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + hydrogen sulfide + NAD(+) = ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29919, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:139151; EC=2.4.2.59;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00304};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00304};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00304}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00304}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00304}.
CC   -!- CAUTION: Despite the fact that this protein belongs to a subfamily
CC       proposed to have ribose 1,5-bisphosphate isomerase activity
CC       (PubMed:15375115), the recombinant protein does not possess this
CC       activity (PubMed:17303759). In contrast, another protein from
CC       P.kodakaraensis has been shown to display this activity (TK0185).
CC       {ECO:0000305|PubMed:17303759}.
DR   EMBL; AP006878; BAD84623.1; -; Genomic_DNA.
DR   RefSeq; WP_011249389.1; NC_006624.1.
DR   SMR; Q5JD25; -.
DR   STRING; 69014.TK0434; -.
DR   EnsemblBacteria; BAD84623; BAD84623; TK0434.
DR   GeneID; 3234250; -.
DR   KEGG; tko:TK0434; -.
DR   PATRIC; fig|69014.16.peg.426; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   InParanoid; Q5JD25; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; TKOD69014:G1G2A-430-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00304; Thi4; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR002922; Thi4_fam.
DR   InterPro; IPR022828; Thi4_prok.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00292; TIGR00292; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Iron; Metal-binding; NAD; Reference proteome;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN         1    251       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000153954.
FT   NP_BIND      53     54       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   NP_BIND     151    153       NAD; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       153    153       Iron; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       168    168       Iron. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      34     34       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      61     61       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     125    125       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     216    216       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     226    226       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   251 AA;  26641 MW;  E43CCF608C7CB1D7 CRC64;
     MREIEISRAI VEAYFNDLLQ NLQLDIAIVG AGPSGMVAGY YLAKGGAKVA IFEKKLSVGG
     GIWGGAMGFN RVVVQESARE ILDEFGVDYS QVGNGLYVLD SIELASTLAS KAVKAGAKIF
     NMVEVEDLVV KDGRVSGLVI NWTPVMMTGL HVDPLTVEAK FVVDSTGHGA QISQHLLKRG
     LIKAIPGEGP MWAEKGEELT VEHTREVFPG LYATGMAANA LAGAPRMGPI FGGMLLSGRK
     AALEILQKLG K
//
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