ID G8P835_LACLC Unreviewed; 658 AA.
AC G8P835;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=llh_4370 {ECO:0000313|EMBL:AEU40050.1};
OS Lactococcus cremoris subsp. cremoris A76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1104322 {ECO:0000313|EMBL:AEU40050.1, ECO:0000313|Proteomes:UP000007114};
RN [1] {ECO:0000313|EMBL:AEU40050.1, ECO:0000313|Proteomes:UP000007114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A76 {ECO:0000313|EMBL:AEU40050.1,
RC ECO:0000313|Proteomes:UP000007114};
RA Bolotin A., Quinquis B., Ehrlich S.D., Sorokin A.;
RT "Complete Genome Sequence of Lactococcus lactis subsp. cremoris A76.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP003132; AEU40050.1; -; Genomic_DNA.
DR RefSeq; WP_014572305.1; NC_017492.1.
DR AlphaFoldDB; G8P835; -.
DR KEGG; llr:llh_4370; -.
DR PATRIC; fig|1104322.3.peg.876; -.
DR HOGENOM; CLU_009227_0_0_9; -.
DR Proteomes; UP000007114; Chromosome.
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 351..522
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 658 AA; 71758 MW; 58F32CD702695946 CRC64;
MFDTTDQLAV NTIRTLSLDA IQKANSGHPG LPMGSAPMAY VLWSKFLNVN PKTSRKWSNR
DRFVLSAGHG SAMLYSLLHL AGYNVTTDDL KGFRQWQSKT PGHPEVNHTD GVEATTGPLG
QGIANSVGMA MAEAHLAAQY NKPGFDIVDH YTYALNGDGD LMEGVSQEAA SLAGKLKLGK
LILFYDSNNI SLDGDLSMSF IDDIQKRFES YGWQHLLVKD GNDLEEIAAA VEVAKAEKSK
PTIIEVKTVI GFGAEKQGTS AVHGAPLGAD GVAFAKKAYG WDYPEFTVPE EVSKRFLETT
VARGEAMEQV WRSTFDDYSE KYPELAEQYV KAFENETPEL TLTKHEMETS KASRVTSQEA
IQELSAQMPN LWGGSADLSA SNNTMVKVEE DFMPDNYVGR NIWFGVREFA MGAIMNGIAL
HGGTRVYGGT FFVFSNYMLP SVRMAALQSL PVTYVWTHDS IAVGEDGPTH EPVEQLASVR
SIPNLDVIRP ADGNEVVAAW RRAASSKSRP TALILTRQNL PVLPDTYELA EEGLNRGAYI
LSKEEGKLEG IIIATGSEVA LALEAKKTLG SGIRVVSMPS MNIFDEQSAD YREEILPKSV
RRRLAIEAGT SYGWGKYVGL DGATVTVDTW GASAPANIVL PAYGFTAENV IKVYQSLD
//
