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Database: UniProt
Entry: THI4_SULAC
LinkDB: THI4_SULAC
Original site: THI4_SULAC 
ID   THI4_SULAC              Reviewed;         265 AA.
AC   Q4JAF8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-JUL-2019, entry version 87.
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=Saci_0854;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 /
OS   NBRC 15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80221.1; -; Genomic_DNA.
DR   RefSeq; WP_011277723.1; NC_007181.1.
DR   SMR; Q4JAF8; -.
DR   STRING; 330779.Saci_0854; -.
DR   EnsemblBacteria; AAY80221; AAY80221; Saci_0854.
DR   GeneID; 3472725; -.
DR   KEGG; sai:Saci_0854; -.
DR   PATRIC; fig|330779.12.peg.818; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; SACI330779:G1G4L-837-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001018; 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    265       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000300739.
FT   NP_BIND      62     63       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   NP_BIND     162    164       NAD; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       164    164       Iron; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       179    179       Iron. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      43     43       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      70     70       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     134    134       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     229    229       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     239    239       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   265 AA;  28388 MW;  C1D84D14A0148EB4 CRC64;
     MSDSIKIKAI DEVKISRYII KQTMEDWMNF VENDVVIVGA GPAGMSAAYY LAKHGLKTLV
     FERRLSFGGG IGGGAMLFHK LVIESPADEV LKEMNIRLEK VEDGVYIVDS AEFMAKLAAS
     AIDAGAKIIH GVTVDDVIFR ENPLRVAGVA VEWTATQMAG LHVDPVFISA KAVVDATGHD
     AEVVAVASRK IPELGIVIPG ERSAYSEMAE KLTVEQTGVV APGLYVAGMS VTEVRGLPRM
     GPIFGSMVLS GKKVAEDIIK DLRNS
//
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