ID A0A367Y580_9ASCO Unreviewed; 585 AA.
AC A0A367Y580;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Transketolase 1 {ECO:0000313|EMBL:RCK61025.1};
DE Flags: Fragment;
GN Name=TKT1_1 {ECO:0000313|EMBL:RCK61025.1};
GN ORFNames=Cantr_07974 {ECO:0000313|EMBL:RCK61025.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK61025.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK61025.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK61025.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RCK61025.1}.
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DR EMBL; QLNQ01000026; RCK61025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Y580; -.
DR STRING; 5486.A0A367Y580; -.
DR Proteomes; UP000253472; 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; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-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:UP000253472};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 326..496
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 585
FT /evidence="ECO:0000313|EMBL:RCK61025.1"
SQ SEQUENCE 585 AA; 63176 MW; 62C22989DD30DF20 CRC64;
MPSIDELAIS TIRGLAVDAV ASANSGHPGA PLGLAPAAHV VWKQMNFNPK DPNWINRDRF
VLSNGHACAL LYSLLVLYGY DLTVDDLKQF RQLGSKTPGH PEATDTPGVD VTTGPLGQGI
SNAVGIAIAQ KQFAATYNKD DIKLSDSYVY AFVGDGCLME GVSSEASSLA GHLQLNNLIA
FWDDNRISID GDTAVSFTEN VPERYRAYGW NVLEVEEGDT DLEGIAKAIE EAKKTTDKPT
LIRLRTIIGY GSLKQGTHDV HDEVAKFYAD EVAKKQKTQA AWDAKFAEYK QKYPEAGAEV
QRRLDGKLPD NWRQHLPTYT PADKPLATRK LSENVINALH GHIPEFIGGS ADLTGSNLTR
ATGSVDFQPP STGLGDYDGV YIRYGVREHG MGAIMNGIAA FGANYKNYGG TFLNFVSYAA
GALRLSALSH HPVIWVATHD SIGLAYPETL AHFRAIPNLS VWRPADGNEV SGAYAAAIES
TDHPSVIALT RQNLPQLEGS SIENTLKGGY TLVKQDKPDV IIVSSGSEVS ISVGAAEVLS
KQGVKANVVS LPDFFTFDKQ SYEYRKSVLP DGVPILSVEV MTTFG
//
