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Database: UniProt
Entry: B2VQD8_TRIHA
LinkDB: B2VQD8_TRIHA
Original site: B2VQD8_TRIHA 
ID   B2VQD8_TRIHA            Unreviewed;       322 AA.
AC   B2VQD8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   03-JUL-2019, entry version 44.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000256|HAMAP-Rule:MF_03158};
DE   AltName: Full=Thiazole biosynthetic enzyme {ECO:0000256|HAMAP-Rule:MF_03158};
DE            EC=2.4.2.60 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   Name=Thi4 {ECO:0000313|EMBL:ABG46357.1};
GN   ORFNames=CI102_502 {ECO:0000313|EMBL:PKK54844.1}, THAR02_01412
GN   {ECO:0000313|EMBL:KKP06454.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:ABG46357.1};
RN   [1] {ECO:0000313|EMBL:ABG46357.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Qian Y.;
RT   "Cloning and expression of thiazole biosynthetic enzyme from
RT   Trichoderma harzianum.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PKK54844.1, ECO:0000313|Proteomes:UP000233603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TR274 {ECO:0000313|EMBL:PKK54844.1,
RC   ECO:0000313|Proteomes:UP000233603};
RX   PubMed=24635846; DOI=10.1186/1471-2164-15-204;
RA   Steindorff A.S., Ramada M.H., Coelho A.S., Miller R.N.,
RA   Pappas G.J.Jr., Ulhoa C.J., Noronha E.F.;
RT   "Identification of mycoparasitism-related genes against the
RT   phytopathogen Sclerotinia sclerotiorum through transcriptome and
RT   expression profile analysis in Trichoderma harzianum.";
RL   BMC Genomics 15:204-204(2014).
RN   [3] {ECO:0000313|EMBL:KKP06454.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|EMBL:KKP06454.1};
RA   Baroncelli R., Vannacci G.;
RT   "The genome sequence of Trichoderma harzianum T6776.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma
RT   harzianum T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
RN   [5] {ECO:0000313|EMBL:PKK54844.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TR274 {ECO:0000313|EMBL:PKK54844.1};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_03158}.
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:0000256|HAMAP-Rule:MF_03158};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03158};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03158}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-211 to a reaction intermediate, generating a dehydroalanine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
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DR   EMBL; DQ647956; ABG46357.1; -; mRNA.
DR   EMBL; JOKZ01000025; KKP06454.1; -; Genomic_DNA.
DR   EMBL; NQLC01000007; PKK54844.1; -; Genomic_DNA.
DR   EnsemblFungi; KKP06454; KKP06454; THAR02_01412.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
DR   Proteomes; UP000233603; Unassembled WGS sequence.
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   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000034112,
KW   ECO:0000313|Proteomes:UP000233603};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03158};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      105    106       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      290    292       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      84     84       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     113    113       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     178    178       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     213    213       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     228    228       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     280    280       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     211    211       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   322 AA;  34547 MW;  E1580FEFFD293391 CRC64;
     MSPPAAVSPT QHTAELVKPV SKLAVAQNQG PLAKTVSEMH GQWDSFTFAP IRESQVSRAM
     TRRYFEDLDN YAESDIVIIG AGSCGLSTAY VLGTQRPDLK IAIIEASVSP GGGAWLGGQL
     FSAMVMRKPA DAFLREIGVP YEDEGNYVVV KHAALFTSTI MAKVLQLPNV KLFNATCVED
     LITRPSAEGV RIAGVVTNWT LVSMHHDDQS CMDPNTINAP LVISTTGHDG PMGAFCVKRL
     VSMGRIEKLG GMRGLDMNRA EDAIVKNTRE VVPGLIVGGM ELSEIDGANR MGPTFGAMAL
     SGVKAAEEAL KVFETRRKEN AI
//
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