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Database: UniProt
Entry: F0S286_DESTD
LinkDB: F0S286_DESTD
Original site: F0S286_DESTD 
ID   F0S286_DESTD            Unreviewed;       264 AA.
AC   F0S286;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   03-JUL-2019, entry version 51.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000256|HAMAP-Rule:MF_00304};
DE            EC=2.4.2.59 {ECO:0000256|HAMAP-Rule:MF_00304};
GN   Name=thi4 {ECO:0000256|HAMAP-Rule:MF_00304};
GN   OrderedLocusNames=Dester_1473 {ECO:0000313|EMBL:ADY74101.1};
OS   Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC   Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
OC   Desulfurobacterium.
OX   NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY74101.1, ECO:0000313|Proteomes:UP000007102};
RN   [1] {ECO:0000313|EMBL:ADY74101.1, ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX   PubMed=22675590; DOI=10.4056/sigs.2465574;
RA   Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S.,
RA   Deshpande S., Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Han C., Land M., Hauser L., Pan C.,
RA   Brambilla E.M., Rohde M., Spring S., Sikorski J., Wirth R.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer
RT   Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a
RT   deep-sea hydrothermal vent.";
RL   Stand. Genomic Sci. 5:407-415(2011).
RN   [2] {ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfurobacterium thermolithotrophum DSM
RT   11699.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00304};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00304};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00304}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00304}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00304}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00304}.
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DR   EMBL; CP002543; ADY74101.1; -; Genomic_DNA.
DR   RefSeq; WP_013639049.1; NC_015185.1.
DR   STRING; 868864.Dester_1473; -.
DR   EnsemblBacteria; ADY74101; ADY74101; Dester_1473.
DR   KEGG; dte:Dester_1473; -.
DR   eggNOG; ENOG4105IQJ; Bacteria.
DR   eggNOG; COG1635; LUCA.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 1025532at2; -.
DR   BioCyc; DTHE868864:G1GRT-1517-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000007102; 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 {ECO:0000313|Proteomes:UP000007102};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007102};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      56     57       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       160    160       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       175    175       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      37     37       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      64     64       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     160    160       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     229    229       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     239    239       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   264 AA;  28547 MW;  13187A27357A4A2D CRC64;
     MQNLNEVVIS QAIIESYMEK LKDHLEVDVA IVGGGPSGLV AGYYLAKEGF KVSIYERRIS
     IGGGMWAGAM FFNEIVVQEM GREIFDEFEV NYKEFKPGYY LADAVEAVTT IASKAVKAGA
     VIFNGMTAED VVLKKVNGNY RVCGLVINWS TVEMNHLMVD PLVITSKYVI DATGHDATVV
     STLQRKAGVK LATETGCVVG EKPLWASVGE EDTVKNSREV FPGIYVSGMA ANATCGSHRM
     GPVFGGMLMS GKKVAQEIAK KLRG
//
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