THI4_FUSOX
ID THI4_FUSOX Reviewed; 320 AA.
AC P23618;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 104.
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;
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=f. sp. cucumerinum / Isolate B1-GK;
RX PubMed=2376567; DOI=10.1128/jb.172.8.4522-4528.1990;
RA Choi G.H., Marek E.T., Schardl C.L., Richey M.G., Chang S., Smith D.A.;
RT "sti35, a stress-responsive gene in Fusarium spp.";
RL J. Bacteriol. 172:4522-4528(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-57, INDUCTION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=f. sp. cucumerinum / F9;
RX PubMed=16232860; DOI=10.1016/s1389-1723(00)80085-7;
RA Akiyama K., Thanonkeo P., Ogawa H., Ohguchi T., Takata R.;
RT "Detection and cloning of the gene encoding a protein produced by
RT nonpathogenic mutants of Fusarium oxysporum.";
RL J. Biosci. Bioeng. 90:302-307(2000).
CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole.
CC Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-
CC (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an
CC adenylated thiazole intermediate. The reaction includes an iron-
CC dependent sulfide transfer from a conserved cysteine residue of the
CC protein to a thiazole intermediate. The enzyme can only undergo a
CC single turnover, which suggests it is a suicide enzyme. May have
CC additional roles in adaptation to various stress conditions and in DNA
CC damage tolerance. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP-
CC thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-
CC carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708,
CC Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873,
CC ChEBI:CHEBI:139151; EC=2.4.2.60; Evidence={ECO:0000255|HAMAP-
CC 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-Rule:MF_03158};
CC -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03158}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mycelia but not in yeast-form cells.
CC Expressed during plant infection. {ECO:0000269|PubMed:16232860}.
CC -!- INDUCTION: Repressed by thiamine. Induced by ethanol, Cu(2+) chloride
CC and heat. {ECO:0000269|PubMed:16232860}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 209 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M33643; AAA33341.1; -; mRNA.
DR EMBL; AB033416; BAA85305.1; -; Genomic_DNA.
DR PIR; B37767; B37767.
DR AlphaFoldDB; P23618; -.
DR SMR; P23618; -.
DR VEuPathDB; FungiDB:FOC1_g10008179; -.
DR VEuPathDB; FungiDB:FOC4_g10009273; -.
DR VEuPathDB; FungiDB:FOIG_10807; -.
DR VEuPathDB; FungiDB:FOMG_07196; -.
DR VEuPathDB; FungiDB:FOXG_10428; -.
DR VEuPathDB; FungiDB:FOZG_09902; -.
DR VEuPathDB; FungiDB:HZS61_002986; -.
DR OMA; MWGGGMM; -.
DR PhylomeDB; P23618; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Iron; Metal-binding; NAD; Nucleus;
KW Stress response; Thiamine biosynthesis; Transferase.
FT CHAIN 1..320
FT /note="Thiamine thiazole synthase"
FT /id="PRO_0000034054"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 288..290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT MOD_RES 209
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="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
