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Database: UniProt
Entry: THI4_SULTO
LinkDB: THI4_SULTO
Original site: THI4_SULTO 
ID   THI4_SULTO              Reviewed;         266 AA.
AC   Q975R0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-JUL-2019, entry version 104.
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};
GN   OrderedLocusNames=STK_03610;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 /
OS   7) (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M.,
RA   Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S.,
RA   Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y.,
RA   Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T.,
RA   Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic
RT   Crenarchaeon, Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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}.
DR   EMBL; BA000023; BAB65340.1; -; Genomic_DNA.
DR   RefSeq; WP_010978323.1; NC_003106.2.
DR   SMR; Q975R0; -.
DR   STRING; 273063.STK_03610; -.
DR   EnsemblBacteria; BAB65340; BAB65340; STK_03610.
DR   GeneID; 1458284; -.
DR   KEGG; sto:STK_03610; -.
DR   PATRIC; fig|273063.9.peg.420; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; STOK273063:G1G3D-432-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001015; 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    266       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000300741.
FT   NP_BIND      63     64       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   NP_BIND     163    165       NAD; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       165    165       Iron; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       180    180       Iron. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      44     44       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      71     71       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     135    135       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     230    230       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     240    240       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   266 AA;  28473 MW;  B8584E4825C17770 CRC64;
     MDSNSIKVKQ VDEVKISKYI LKYTFQDWED IVESDVVIVG AGPSGMTAAY YLAKAGLKTV
     VFERRLSFGG GIGGGAMLFH KIVIESPADE ILKEMKIKLN KVEEGVYIVD SAEFMAKLAA
     SAIDAGAKII HGVTVDDVIF RENPLKVVGV AVEWTATQMA GLHVDPLFIS AKAVVDATGH
     DAEVISVAAR KIPELNIVIP GEKSAYSETA EELTVENTGM VAPGLYAAGM AVTEVKGLPR
     MGPIFGAMVL SGKRVAEIII KDLRYS
//
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