ID A0A0R2GSW1_9LACO Unreviewed; 662 AA.
AC A0A0R2GSW1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=IV41_GL000990 {ECO:0000313|EMBL:KRN43953.1};
OS Limosilactobacillus ingluviei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN43953.1, ECO:0000313|Proteomes:UP000051639};
RN [1] {ECO:0000313|EMBL:KRN43953.1, ECO:0000313|Proteomes:UP000051639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN43953.1,
RC ECO:0000313|Proteomes:UP000051639};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN43953.1}.
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DR EMBL; JQBA01000027; KRN43953.1; -; Genomic_DNA.
DR RefSeq; WP_056994659.1; NZ_JQBA01000027.1.
DR AlphaFoldDB; A0A0R2GSW1; -.
DR PATRIC; fig|148604.4.peg.1030; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000051639; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051639};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 349..520
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 662 AA; 72192 MW; A0D5252C656BDD49 CRC64;
MSYSAIDHLA VNTIRALSMD TITHAKSGHT GITLSAAPLL YVIYKNMHVD TTDPHWFGRD
RFVLSGGHGS AMLYSLLHLI GYDLSIDDLK HFRTLDSKTP GHPEITTPGV DAATGPLGQG
FATAVGMAMA AKHLAAIYNR PGYPVIDNRI YVEAGDGDLM EGISHEAASL AGHLRLNNLI
VLLDSNRNTM DSLLSDESND NVAERFKAYG WNYLVVEDGN DLEAIDAAVQ IAKDEQTRPT
LIEVKTTLGY ASPLADSHKA HGTVLTAEQV QATKANLNYQ AAPFAVPEEV YAHFQQLRQR
GQAAHKAWDD LMAKYAKAFS QQAQNLQANL THAVKFDATK LAPDFAENEA TRDAIHQLLQ
VTAEQSELNL WGGSADLGSS DKTYLDADKG FQPDRYDQKN IAFGIREFAE GAALNGIALY
GGSRAYGNTF LIFSEYMRSA IRSAALMDLP TLYLFGHDSI SLGPDGPTHQ PIEQLAGFRA
MPNLTVFRPA DALETMYAWE TALNQQHPVL MALGRQKLPT LFKYQDAVKQ GVPKGGYILS
EAANNEPSGI LMGTGSEVAL LLAAQAQLAT DNIFVRVVSM PSFELFKAQP QAYRDEVLPP
VLRQRLSVEM ATTDDWAQFV GLDGVSIGID HFGASGNGDD LIKRSGFTVE NIVGQYKQNF
LK
//
