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Database: UniProt
Entry: D4AUM3_ARTBC
LinkDB: D4AUM3_ARTBC
Original site: D4AUM3_ARTBC 
ID   D4AUM3_ARTBC            Unreviewed;       341 AA.
AC   D4AUM3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   03-JUL-2019, entry version 45.
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   ORFNames=ARB_07940 {ECO:0000313|EMBL:EFE33188.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
OS   (Trichophyton mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE33188.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K.,
RA   Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W.,
RA   Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C.,
RA   Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F.,
RA   Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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-230 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFE33188.1}.
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DR   EMBL; ABSU01000011; EFE33188.1; -; Genomic_DNA.
DR   RefSeq; XP_003013828.1; XM_003013782.1.
DR   STRING; 63400.XP_003013828.1; -.
DR   EnsemblFungi; EFE33188; EFE33188; ARB_07940.
DR   GeneID; 9521246; -.
DR   KEGG; abe:ARB_07940; -.
DR   eggNOG; KOG2960; Eukaryota.
DR   eggNOG; COG1635; LUCA.
DR   KO; K03146; -.
DR   Proteomes; UP000008866; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008866};
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:UP000008866};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      118    119       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      309    311       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      97     97       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     126    126       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     194    194       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     232    232       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     247    247       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     299    299       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     230    230       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   341 AA;  36305 MW;  518CBAF965656FBE CRC64;
     MAPPPTATLT ETVASVGNVV RDNFAGEGNT LAQAAPEAGS GSGSGYALLD DFAGKWEEFK
     FAPIRESQVS RAMTSRYFKD MDTYAESDIV IVGAGSCGLS TAYVLGKARP DLKIALIEAS
     VSPGGGAWLG GQLFSAMVLR KPAHRFLDDL GVPYEEDASN PNLVVIKHAA LFTSTLLSKV
     LSFPNIKLFN ATCVEDLITR PRASEASGFQ IAGVVTNWTL VTQHHDDHSC MDPNTINAPL
     IISTTGHDGP FGAFCAKRLV SMSALEKLGG MKGLDMNSAE EAIVKNTREV TKGLIIGGME
     LSEIDGWHRM GPIFSAMMLS GLKAAEVALE VFEERKKECS A
//
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