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THI4_ASPFU
ID   THI4_ASPFU              Reviewed;         332 AA.
AC   Q4WMX7;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158};
GN   Name=thiA {ECO:0000255|HAMAP-Rule:MF_03158}; ORFNames=AFUA_6G08360;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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   -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC       221 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}.
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DR   EMBL; AAHF01000006; EAL88687.1; -; Genomic_DNA.
DR   RefSeq; XP_750725.1; XM_745632.1.
DR   AlphaFoldDB; Q4WMX7; -.
DR   SMR; Q4WMX7; -.
DR   STRING; 746128.CADAFUBP00007239; -.
DR   PRIDE; Q4WMX7; -.
DR   EnsemblFungi; EAL88687; EAL88687; AFUA_6G08360.
DR   GeneID; 3508853; -.
DR   KEGG; afm:AFUA_6G08360; -.
DR   VEuPathDB; FungiDB:Afu6g08360; -.
DR   eggNOG; KOG2960; Eukaryota.
DR   HOGENOM; CLU_053727_0_0_1; -.
DR   InParanoid; Q4WMX7; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
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   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; NAD; Nucleus; Reference proteome;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..332
FT                   /note="Thiamine thiazole synthase"
FT                   /id="PRO_0000415876"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         108..109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   BINDING         300..302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT   MOD_RES         221
FT                   /note="2,3-didehydroalanine (Cys)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
SQ   SEQUENCE   332 AA;  35492 MW;  3F70D7BA8543D00F CRC64;
     MSPPAAIFEP AVAPSPSLKA KVLVPETVPA SGTSQTHLLD HFGGKWDDFK FAPIRESQVS
     RAMTRRYFQD LDKYAESDIV IVGAGSCGLS TAYVLAKARP DLKIAIIEAS VSPGGGAWLG
     GQLFSAMVLR RPAEVFLNEI GVPFEEDPAN PNFVVVKHAS LFTSTLMSKV LSFPNVKLFN
     ATAVEDLVTR PSASGDAKDT QIAGVVVNWT LVTLHHDDHS CMDPNTINAP VVISTTGHDG
     PFGAFCAKRL VSMNTVDKLG GMRGLDMNSA EDAIVKNTRE VAKGLIIGGM ELSEIDGFNR
     MGPTFGAMVL SGVKAAEEAL KVFDQRQREC AE
 
 
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