ID A0A0J7Z3U9_STRVR Unreviewed; 701 AA.
AC A0A0J7Z3U9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=ACM01_32945 {ECO:0000313|EMBL:KMS69898.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS69898.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS69898.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS69898.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-2015) 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}.
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:KMS69898.1}.
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DR EMBL; LFNT01000053; KMS69898.1; -; Genomic_DNA.
DR RefSeq; WP_048585088.1; NZ_LGUR01000252.1.
DR AlphaFoldDB; A0A0J7Z3U9; -.
DR PATRIC; fig|1938.3.peg.6713; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000037432; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 371..555
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 701 AA; 75513 MW; A41F4CBA7355ECDF CRC64;
MSTKPTTTDL EWTELDQRAV DTARVLAADA VQKVGNGHPG TAMSLAPAAY TLFQKVMRHD
PADADWVGRD RFVLSAGHSS LTLYTQLYLA GFGLELDDLK AFRTWGSKTP GHPEYGHTTG
VETTTGPLGQ GVANAVGMAM AARYERGLFD PEAAEGTSPF DHFVYVIAGD GCLQEGISAE
ASSLAGHQKL GNLVLLWDDN HISIEGDTET AVSEDTVKRY EAYGWHVQRV EPQANGDLDP
AAIYDAIQQA KAVTDKPSFI AMRSIIAWPA PNAQNTEAAH GSALGDDEVA ATKRVLGFDP
EQSFEVADEV IEHTRGALER GQAARAVWEK SFQQWRDNNP ERAAEFDRIS KGELPTGWEE
KIPVFEPGKG VATRAASGKI LQALGAVIPE LWGGSADLAG SNNTTIDKTS SFLPADNPLP
EADPYGRTIH FGIREHSMAA EMNGIALHGN TRIYGGTFLV FSDYMRNAVR LSALMHLPVT
YVWTHDSIGL GEDGPTHQPI EHLASLRAIP GLNVVRPADA NETAIAWREI LSRYTKEFGK
GAPHGLALTR QGVPTYEPNE DAAKGGYVLF EASNGTPEVV LIATGSEVHV AVEARERLEA
DGVPTRVVSM PSVEWFEEQD QGYRDSVLPP AVKARVAVEA GIGLTWHKYV GDAGRIVSLE
HFGASADGKV LFREYGFTAE NVAAVARAVL DSTTGLAAAQ R
//
