GenomeNet

Database: UniProt
Entry: THI4_FUSO4
LinkDB: THI4_FUSO4
Original site: THI4_FUSO4 
ID   THI4_FUSO4              Reviewed;         320 AA.
AC   J9N5G7;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-JUL-2019, entry version 49.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_03158};
DE            EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_03158};
DE   AltName: Full=Stress-inducible protein sti35;
DE   AltName: Full=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158};
GN   Name=sti35; ORFNames=FOXG_10428;
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC
OS   9935 / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
RA   Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
RA   Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
RA   Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
RA   Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
RA   Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
RA   Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
RA   Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
RA   Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
RA   Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
RA   Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
RA   Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
RA   Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [2]
RP   FUNCTION.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RX   PubMed=17964830; DOI=10.1016/j.fgb.2007.09.003;
RA   Ruiz-Roldan C., Puerto-Galan L., Roa J., Castro A., Di Pietro A.,
RA   Roncero M.I., Hera C.;
RT   "The Fusarium oxysporum sti35 gene functions in thiamine biosynthesis
RT   and oxidative stress response.";
RL   Fungal Genet. Biol. 45:6-16(2008).
CC   -!- FUNCTION: Involved in biosynthesis of the thiamine precursor
CC       thiazole. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid
CC       (ADT), an adenylated thiazole intermediate. The reaction includes
CC       an iron-dependent sulfide transfer from a conserved cysteine
CC       residue of the protein to a thiazole intermediate. The enzyme can
CC       only undergo a single turnover, which suggests it is a suicide
CC       enzyme. May have additional roles in adaptation to various stress
CC       conditions and in DNA damage tolerance. {ECO:0000255|HAMAP-
CC       Rule:MF_03158, ECO:0000269|PubMed:17964830}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) =
CC         [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + 2 H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55708, Rhea:RHEA-COMP:14264, Rhea:RHEA-
CC         COMP:14265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, ChEBI:CHEBI:139151;
CC         EC=2.4.2.60; Evidence={ECO:0000255|HAMAP-Rule:MF_03158};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03158};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03158};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_03158}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-209 to a reaction intermediate, generating a dehydroalanine
CC       residue. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03158}.
DR   EMBL; AAXH01000627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018248086.1; XM_018389758.1.
DR   RefSeq; XP_018248087.1; XM_018389759.1.
DR   RefSeq; XP_018248088.1; XM_018389760.1.
DR   RefSeq; XP_018248089.1; XM_018389761.1.
DR   RefSeq; XP_018248090.1; XM_018389762.1.
DR   RefSeq; XP_018248091.1; XM_018389763.1.
DR   RefSeq; XP_018248092.1; XM_018389764.1.
DR   SMR; J9N5G7; -.
DR   PRIDE; J9N5G7; -.
DR   EnsemblFungi; FOXG_10428T0; FOXG_10428P0; FOXG_10428.
DR   GeneID; 28951907; -.
DR   KEGG; fox:FOXG_10428; -.
DR   KO; K03146; -.
DR   OMA; MWGGGMM; -.
DR   Proteomes; UP000009097; Chromosome 7.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_03158; THI4; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027495; Sti35.
DR   InterPro; IPR002922; Thi4_fam.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00292; TIGR00292; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Iron; Metal-binding; NAD; Nucleus;
KW   Reference proteome; Thiamine biosynthesis; Transferase.
FT   CHAIN         1    320       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000423475.
FT   REGION      103    104       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      288    290       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      82     82       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     111    111       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     176    176       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     211    211       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     226    226       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     278    278       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   MOD_RES     209    209       2,3-didehydroalanine (Cys).
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   320 AA;  34579 MW;  2287B18F266E2142 CRC64;
     MAPPAAVSPP SRSAELATST KLPVMSKNIN TKTVEEMLGQ WDDFKFAPIR ESQVSRAMTR
     RYFQDLDNYA ESDIVIIGAG SCGLSAAYIL GKKRPDLKIA IIEASVSPGG GAWLGGQLFS
     AMIMRKPADA FLREVGVPYE DEGNYVVVKH AALFTSTIMS KVLQMPNIKL FNATCVEDLI
     TRPSEEGVRI AGVVTNWTLV SMHHDDQSCM DPNTINAPLI ISTTGHDGPM GAFCVKRLVS
     MQRIEKLGGM RGLDMNLAED AIVKGTREIV PGLIVGGMEL SEVDGANRMG PTFGAMALSG
     LKAAEEALKI FDTRKKQNDL
//
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