ID A0A2P8B0A0_9ACTN Unreviewed; 712 AA.
AC A0A2P8B0A0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:PSK66148.1};
GN ORFNames=B0E53_01892 {ECO:0000313|EMBL:PSK66148.1};
OS Micromonospora sp. MH33.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1945509 {ECO:0000313|EMBL:PSK66148.1, ECO:0000313|Proteomes:UP000240342};
RN [1] {ECO:0000313|EMBL:PSK66148.1, ECO:0000313|Proteomes:UP000240342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH33 {ECO:0000313|EMBL:PSK66148.1,
RC ECO:0000313|Proteomes:UP000240342};
RA Thatcher L.F., Myers C.A., O'Sullivan C.A., Roper M.;
RT "Draft genome sequences of Micromonospora sp. MH33 and MH99.";
RL Submitted (FEB-2017) 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:PSK66148.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUYZ01000040; PSK66148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8B0A0; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000240342; 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:UP000240342};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PSK66148.1}.
FT DOMAIN 379..559
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 712 AA; 77098 MW; E00A594905DC1920 CRC64;
MAANRPELPA LNWSDLDRRA VDTVRVLAMD AVEKSGNGHP GTAMSLAPAA YLLFNRVMRH
NPADPNWSGR DRFVLSAGHS SLTLYIQLFL SGYPLALDDL KALRQWGSLT PGHPEHGHTP
GVETTTGPLG QGLGNAVGMA MAARRERGLF DPEPERGDSP FDHDIWCIAS DGDIEEGISH
EVSALAGHQQ LGNLCVIYDD NEISIEDDTR IAKSEDVAAR YAAYGWHVQT VDWRRGDADQ
GDYHEDVEAL HQALLAARAE TGRPSFIALR TIIGWPAPNK QNTGKIHGSA LGADEVKATK
RILGFDPERT FEIDDEVLKH ARQVMDRGAE AQAAWTTTFD AWARANPERK ALWDRMSTRT
LPQGWTDALP TFPADAKGIA TRAASGKVLE ALAPVLPELW GGSADLAESN NTTMKGEPSF
IPAEHATKDF PGDEYGRTLH FGIREHAMGA ILNGIALHGG TRPYGGTFLV FSDYMRPSVR
LAALMKLPVT YVWTHDSIGL GEDGPTHQPV EHLTALRAIP GLDVVRPADA NETAWAWRQA
LEHTDRPTAL ALSRQALPTL DRTDLAGAEG VAKGGYVLAE ASTGKPQVII VGTGSEVQLC
LTARERLEAD GTPTRVVSMP CQEWFFAQDE AYRESVLPRG VKARVSVEAG IAMSWRAIVG
DSGECVSLEH YGASAPHTVL FEQFGFTPDR IVAAAHAALT RVGDITGFTT GN
//
