ID D7GS30_9FIRM Unreviewed; 660 AA.
AC D7GS30;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, 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=CK3_08400 {ECO:0000313|EMBL:CBL40606.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL40606.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL40606.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40606.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL40606.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40606.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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; FP929062; CBL40606.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GS30; -.
DR KEGG; bprs:CK3_08400; -.
DR PATRIC; fig|245014.3.peg.2572; -.
DR HOGENOM; CLU_009227_0_0_9; -.
DR BioCyc; BBAC245014:G1314-704-MONOMER; -.
DR Proteomes; UP000008961; 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 354..526
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 660 AA; 71570 MW; 90E46C9A97F356AE CRC64;
MNTIDNLAIN SIRILSADAI QKANSGHPGL PLGSAPMAYE LWAHHMNHNP ANPEWANRDR
FILSGGHGSM LLYSLLHLFG YGLTKEDLMN FRQVGSLTPG HPEYGHTVGV EATTGPLGAG
MGMAVGMAMA EKHLASVFNK ESYPVVDHFT YVLGGDGCMM EGISSEAFSL AGTLGLGKLI
VLYDSNRISI EGSTDIAFRE NVEERMKAFG FQTITVEDGT DIDAIGAAIE VAKADTEHPS
FITIKTEIGF GCPAKQGKAS AHGEPLGVDN IKAMRETLGW QYEEPFFVPE EVYEHYSRLA
EEKADVEAAW NAMFAAYCDE YPEMEKLWEQ YHTAPDAKAL IENEALWLTK DKAEATRSLS
GKMINILKDI MPNMIGGSAD LAPSNKTAMK DAGDFSAENP AGRNLHFGVR ELAMTAIGNG
IMLHGGLRAY VATFFVFSDY VKPMARLSAL MGVPLTFVLT HDSIGVGEDG PTHEPIEQLA
MFRAMPNFHV FRPCDATETS AAWLSAVTSE KTPTALVLSR QNLNPIPGSS KDALKGGYVI
DDCEGTPDAI LIASGSEVDL AVKAKAELTA EGKKIRVVSM PCMDIFEEQS AEYKESVLPK
EVRRRIVVEA LSDFGWGKYV GLDGAYVTMK SFGASGPAAK LFEKFGFTVE NVVNTVKTLF
//
