ID   A0A135LMI0_PENPA        Unreviewed;       640 AA.
AC   A0A135LMI0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II {ECO:0000313|EMBL:KXG50154.1};
GN   ORFNames=PGRI_061210 {ECO:0000313|EMBL:KXG50154.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG50154.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG50154.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG50154.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXG50154.1}.
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DR   EMBL; LHQR01000048; KXG50154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LMI0; -.
DR   STRING; 5078.A0A135LMI0; -.
DR   OMA; DMADNTC; -.
DR   OrthoDB; 1691772at2759; -.
DR   Proteomes; UP000070168; 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   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; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   Pyruvate {ECO:0000313|EMBL:KXG50154.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT   DOMAIN          317..492
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   640 AA;  69360 MW;  580715C160BCFE7C CRC64;
     MKGHTFPVDL KQFKQLKLDP KTTQLSPQQK SDLQHNINIF RDAIIAFTAT GSARGVAGHT
     GGPFDTAPEV CILLALMNGN PNKWVDALYD EAGHRVATQY LLAALDGKIE PDHLLNYRAA
     DSHLPGHPEL GFTPGIKFSS GRLGHMWGMV NGIAMANRDK NVIMLGSDGS QQEGNDAEAA
     RIAVANNLNV KLFIDNNDVT IAGHPSQYLK GYEVARTLDG QGLKVLRAQG ENLDSLYGAI
     CEVINHDGPA AVVIDRKMAA GIEGIEGETH AHDVIPVDIA RKYLTKRGYS KEQLAFYDDI
     KPGTNPHTYK GSTKDKGSNR NIFGEAVNDV LDKLSKEEAK RRVMVIDSDL AGSTGLKAIG
     AKHPEAFVAS GVMERGNFSA AAGFGFGSNG ERQGVFSTFS AFLEMCISEI TMARLNDCTV
     LSHFSHSGVD EMADNTCHFG LNHFFADNGL MDAESTALYF PADGEQMKAV VNEVFWKKGL
     RFIFSTRSKV PYILKEGTDQ KLFGEGYKFV PGKEEIIRKG SAGYIVSYGD MLYRSLDAVE
     NLRAEGLDVG LINKPTLNVV DEETIKVYGS SPFVLVVESI AQKTGLGSRL GTHLLERKFT
     PKFKSMGAIK EGCGGLYEQV NAQGLGPSDI IAAVKEVSGN
//