ID A0A0R2LUH2_9LACO Unreviewed; 672 AA.
AC A0A0R2LUH2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN ORFNames=IV54_GL001977 {ECO:0000313|EMBL:KRO03852.1};
OS Levilactobacillus paucivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=616990 {ECO:0000313|EMBL:KRO03852.1, ECO:0000313|Proteomes:UP000051906};
RN [1] {ECO:0000313|EMBL:KRO03852.1, ECO:0000313|Proteomes:UP000051906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22467 {ECO:0000313|EMBL:KRO03852.1,
RC ECO:0000313|Proteomes:UP000051906};
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 -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
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 ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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:KRO03852.1}.
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DR EMBL; JQCA01000052; KRO03852.1; -; Genomic_DNA.
DR RefSeq; WP_057878426.1; NZ_JQCA01000052.1.
DR AlphaFoldDB; A0A0R2LUH2; -.
DR STRING; 616990.IV54_GL001977; -.
DR PATRIC; fig|616990.3.peg.2090; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000051906; 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; 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 Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 362..533
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 672 AA; 72843 MW; 5F73F54392DFD767 CRC64;
MLNEQSAPIK FDDVDTQAVT AVRMLSMDMI SRAHSGHPGL PLGAAPMAYV LFSRHLRVDP
SFPQWFNRDR FVLSAGHGSA MLYSLIHLSG FAITREDLMS FRQLGSKTPG HPEYGVTPGV
DATTGPLGQG IGMAVGMAIA ESHLRGVYNR PDYDVVDHYT YALCGDGDLL EGVAAESASL
AGQLQLNRLI VLYDSNDISL DGPLTNASHD NVGERFQSYG WNYSRVEDGN DLEAIDAAIR
SAKQNAGGPT LIEVKTQIGA GSPKAGTNKV HGAPLSDDEL AATRDFYHWN EDPFTVPEAV
TERFMSTIKA RGWANHQSWS SLIAQYSKAE PDLSRQFAQG VSQTLPDNYA ANVPTYYKKD
ALATRASGSQ VLQQLSKSCP NLWGGSADLF RSNKTAVADE ERFSPTNRQG RNLWFGVREF
AEAAAMNGIA LHGGTRVYGS TFFVFSDYMK PALRLAAIQQ LPVIYVFTHD SLAVGEDGPT
HEPVEQLAAL RSIPNLTVFR PADGNETAAA WEAALETTDH PVALVLTRQA LPTLPLPAAK
VHTGVNQGGY VVRDAKDEAE GILMASGSEV QLALSAQERL AELGHDVRVV SIPSFEAFND
QSHEYQESVL PMKLRRRVAI EMASGSSWYQ FVGLDGVALT QDDFGASGKG EEVIAMAGFT
TDKVVQAYLQ LK
//
