ID A0A0M9WI91_9EURO Unreviewed; 738 AA.
AC A0A0M9WI91;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=ACN38_g3152 {ECO:0000313|EMBL:KOS45913.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS45913.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS45913.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS45913.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS45913.1}.
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DR EMBL; LHQQ01000036; KOS45913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9WI91; -.
DR STRING; 229535.A0A0M9WI91; -.
DR OrthoDB; 5399939at2759; -.
DR Proteomes; UP000037696; 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 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; 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; 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:UP000037696};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 390..573
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 738 AA; 80283 MW; 1BDB3157C16DBE45 CRC64;
MAPALELLEK PAQCLPVKAV SATRNGDAAG LRLESPEKHE RVMNVFRAFI ADLCQQYGEG
HAGSPMGMAA IGISLYKYVM KYSPNNCNYF NRDRFVLSNG HACLWQYLFM HLVGVKSMTL
EQLKSYHSSK LDSVCPGHPE IENEGIEVTT GPLGQGLASA VGLAMATKNL AATYNKPGHE
LVNNMTWCMV GDACLQEGVG LESLSLAGHW KLNNLCVIFD NNSVTCDGTA DVANTEDINT
KMRATGFNVV DVYNGNSDVA EITNALLGAK LSDKPTFLNV RTTIGYGAAK AGTADIHGAA
LGVDEVANFK RRFGLNPDQH FHIPQDVYDF FSDIPGRGAA HEAAWQNALV KYQIEDPVLS
AEFALRVAGK MPEDWTKCIP RTQDQPTAPT ATRKSAGVVT NALAVNINSF LIGTADLTPS
VNVSYKNKVD FQSPELQTAC GLNGDYSGRY IHYGIREHAM CSISNGLSAF NKGTFIPMTS
TYFVFHLYAA AGVRMAALQG LQQIHIATHD SIGVGENGPT HQPIAVAALY RAMPNVLYIR
PCDAEEVAGA YIAAIQATET PTVISLSRQS LTQYPQHSSR EGTLKGAYVF AEAEGDDFDV
TLIGVGSEMG YAMQTRELLL NDHGVRARVV SFPCTRLFEQ QSRDYKQSVL RSRAEKPTVA
IEAYPSNGWE RYADASVSMN SFGKSLPSKE TYEHFGFAPK SIAPKVKALV EEVRRDGIGI
LRGDFRDFNG SLRIGVEH
//