ID   A0A084QX86_STAC4        Unreviewed;       699 AA.
AC   A0A084QX86;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=S40285_06651 {ECO:0000313|EMBL:KFA68571.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA68571.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA68571.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA68571.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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; KL659800; KFA68571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QX86; -.
DR   STRING; 1283841.A0A084QX86; -.
DR   HOGENOM; CLU_009227_0_0_1; -.
DR   InParanoid; A0A084QX86; -.
DR   OMA; DICNQNG; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF6; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          375..548
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   699 AA;  76206 MW;  4C4413BC6D619E46 CRC64;
     MNGHINVSEL QKDLRHSGTD DLQAVKEVRK LVIDICRQNG GGHGGSAIGM APMAVALWKH
     AMRYNPSNTE WFDRDRFVLS NGHAAMLQYV MLHVSGYPHM TTDELKLYGS PKTVDKATKT
     WKSTICHAHP EREVPGIEVT TGPLGQGIAN AVGLAIASKN MAATFNRPGL KIVNSHIYCI
     TGDGCLQEGV ASESASIAGH LGLDNLTLLY DNNQVTCDGP LDWIVSEDTN AKMRSVGWHV
     IDVWDGDTSV ANIASALAQA KLTRGKPTFI NIRTTIGHGT STAGTYKSHH GTYTEEDAAR
     QATNGIASTH TLSEKCRQYW SQVVIRGRDL ESEWNQKMQK YSASFPDLAK VLHQRMTGKI
     DIDFLDMLDV PEAVSATRTF NGTVFNAIME KVPNTMAGGA DLWNSNQMGD QSNRIFDSCH
     PDGRVVRYGI REHAMASISN GIAAYSEGCF IPVTATFFMF YLYAAAGVRM GALSNLKVIH
     VATHDSIGEG QNGPTHQPVE LDSLFRAMPN LLYIRPADSE EVVGAWITAL TADTRPSIIS
     LARDPAGSII KNTNRGKVKK GGYVLVENEK AEVTLISCGS ELQFACEAAT RLTQEGIATR
     VVSMPCIKLF EEQPIEYQVS VLSSSTHVIS VEAYVSSMWA RFCTASVAMD SFGYSGAGRE
     NFARFGIDTD GVVGKVKAAV QEYANKSHEV SSRRWKLLK
//