ID A0A1I5Z190_9PSEU Unreviewed; 706 AA.
AC A0A1I5Z190;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN05421810_108128 {ECO:0000313|EMBL:SFQ50274.1};
OS Amycolatopsis arida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=587909 {ECO:0000313|EMBL:SFQ50274.1, ECO:0000313|Proteomes:UP000198727};
RN [1] {ECO:0000313|Proteomes:UP000198727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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=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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; FOWW01000008; SFQ50274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5Z190; -.
DR STRING; 587909.SAMN05421810_108128; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000198727; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; IPR020826; Transketolase_BS.
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: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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 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:UP000198727};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 378..558
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 706 AA; 75659 MW; C34324A345EE887E CRC64;
MSDTVSTSEN NPLLRRNVPA DWTELDTRAV DTVRVLAADA VEHCGSGHPG TAMSLAPVAY
SLFQRIMRHD PADPEWPARD RFVLSAGHSS LTLYIQLFLA GYGLEMEDLK QLRKWNSRTP
GHPEYRHTPG VETTTGPLGQ GLANAVGMAM AARRERGLLD PDAALGESPF DHHVFVIASD
GDIEEGVTAE ASSLAGRQQL GNLVVIYDDN NISIEDNTDI ALSEDTAKRY EAYGWHVQTV
EGGEDVVAFE EAIAAARAET ARPSFIRLRT IIGYPAPNKM NTGKAHGAAL GADEVAAVKE
ILGFDPDTSF HIDDEVLAHT RQAIDRGKRA RAAWQEQYDQ WAAANPERKE LADRLRTRTL
PEGWAGTLPS WAPDEKGVAT RKASGEVLNT IGDALPELWG GSADLAESNN TIIKNSDSFG
PESASTGMFT AHPYGRNLHF GVREHAMGAV LNGIALHGGT RPYGATFLIF SDYMRPAVRL
AALMKAPVIY VWTHDSIGLG EDGPTHQPIE QLSALRAIPG LNVVRPADAN ETAAAWKAVL
EDVSAPSGLA LTRQNVPVLE GTREKAAEGV ARGGYVLADA ESGTPDVVII ATGSEVQLAV
AARNTLAAEG VAARVVSMPC VEWFDAQSEA YRESVLPSGV KARVAVEAGV AQSWHRFVGD
AGEIVSIEHF GASADYQTLF REFGFTAETV TDAARRSLHT VGSGAA
//
