ID B6H5I8_PENRW Unreviewed; 711 AA.
AC B6H5I8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=Pc14g00180 {ECO:0000313|EMBL:CAP74159.1}, PCH_Pc14g00180
GN {ECO:0000313|EMBL:CAP74159.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP74159.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP74159.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
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}.
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DR EMBL; AM920429; CAP74159.1; -; Genomic_DNA.
DR RefSeq; XP_002560013.1; XM_002559967.1.
DR AlphaFoldDB; B6H5I8; -.
DR STRING; 500485.B6H5I8; -.
DR GeneID; 8307111; -.
DR KEGG; pcs:Pc14g00180; -.
DR VEuPathDB; FungiDB:PCH_Pc14g00180; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR OMA; HTWCMVG; -.
DR OrthoDB; 5399939at2759; -.
DR BioCyc; PCHR:PC14G00180-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c14.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
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; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 378..561
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 711 AA; 77859 MW; B1ED37C47DB405BE CRC64;
MSVEVQQNGV NGVHSSAMPL VHKLSKDHDL VLKTFRLLIA DLCQQFNGGH PGGAIGMAAI
GVALWRYVMR YAPHTPGFFN RDRFVLSNGH TCLFQYSFLH LTGYKAMTFE QLKSYHSDRV
DALCPGHPEI EHEGIEVTTG PLGQGIANAV GLAMATKNLA ATYNRPGFNV VDNHTWCMIG
DACLQEGVGL EAISLAGHFR LNNLTVIYDN NQITCDGSVD LTNTEDVNAK MRACGWDVIE
VADGCFDIEA IVSALEQARS SKEKPTFINI KTVIGLHSSV AGTAVAHGAA FGAQSIRDMK
TAYGFNPEEH FVIGESVRQF FQGIPERGEQ WVQEWDQLVN DYAVQHPDLA AEFKARVRGE
LPPDWEEHIP TAFPDKPTAT RASSGLVFNP IAKDINSFMV GTADLSPSVN MIWPGKVDFQ
HPELRTTCGI NGNYSGRYIH YGVREHAMAA ISNGLAAYSP NTIIPVTSTF FMFYLYAAPA
VRMGALQHLQ IIHVATHDSI GMGEDGPTHQ PIELANLYRA MPNLLYIRPG DSEETAGAWI
AAIGAKQTPS IISTSRQALP QLAQTRRDGV ALGAYVLSEA ESAAVTLIGV GAELSFALEV
AKQLKVQKDI TARVVSFPCQ RLFEKQSLDY KRATLQRHRG IPAVVIEPYA PNGWERYADA
GISVTRFGQS LPGKAAYKFF GYEIATLTTK VASYLERVQE DELLRGEFVD L
//
