TKT2_XANFL
ID TKT2_XANFL Reviewed; 687 AA.
AC Q60103;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transketolase 2 {ECO:0000305};
DE EC=2.2.1.1 {ECO:0000269|PubMed:8550527};
GN Name=cbbT {ECO:0000303|PubMed:8550527};
OS Xanthobacter flavus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=281;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RC STRAIN=H4-14;
RX PubMed=8550527; DOI=10.1128/jb.178.3.888-893.1996;
RA van den Bergh E.R., Baker S.C., Raggers R.J., Terpstra P., Woudstra E.C.,
RA Dijkhuizen L., Meijer W.G.;
RT "Primary structure and phylogeny of the Calvin cycle enzymes transketolase
RT and fructosebisphosphate aldolase of Xanthobacter flavus.";
RL J. Bacteriol. 178:888-893(1996).
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:0000269|PubMed:8550527}.
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:0000269|PubMed:8550527};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P27302};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P27302};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P27302};
CC -!- ACTIVITY REGULATION: Activity is increased sixfold following
CC autotrophic growth on methanol compared with that of heterotrophically
CC grown cells. {ECO:0000269|PubMed:8550527}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; U29134; AAA96741.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60103; -.
DR SMR; Q60103; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
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; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 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; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..687
FT /note="Transketolase 2"
FT /id="PRO_0000441913"
FT ACT_SITE 432
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 87
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 135..137
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 177
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 206
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 282
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 458
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 494
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 541
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT SITE 47
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT SITE 282
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P27302"
SQ SEQUENCE 687 AA; 73236 MW; 791DC70384837457 CRC64;
MTAHAAALAA ADAPAPVDRS PGALGWPVTA ALRALAMDGV EQAKSGHPGA PMGMAEIAAV
LWREHLRHNP ADPSWPDRDR FVLSNGHGSM LIYALLHLTG YDLPIAELKR FRQLHSRTPG
HPELGMTPGV ETTTGPLGQG LANAVGMAIA EKTLAAQFNR PGLSIVDHRT FVFLGDGCLM
EGVSHEACSL AGRLGLGKLV AFYDDNGISI DGKVEEWFPD DTPARFAAYG WHVIRNVDGH
DPAMLRDAVE AALSETGKPT LICCKTTIGR GAPTKEGHQD THGAPLGAEE IARTRAAMGW
DHAPFEVPED IYALWDARRS GAARQSAWDA RMEAYERAYP AEAAEFRRRL KGDLSPAFAA
TYAAALKATV EKAETVATRK ASQLALAALA PAVPEFLGGS ADLAHSNLTT FPGAVPITRD
PAGNQIFYGV REFGMSAIAN GIALHGGFIP FVATFLVFSD YARNAMRMSA LMGQRVIYIL
THDSIGLGED GPTHQPVEHV ESLRLIPNLD VWRPADTVET LAAWHAALTR TNGPSAFILS
RQNLPCWPRD AAQIEGIEAG AYVLRESEGL ARAVLVATGS EVKLAAAAAD LLDTAGIPTR
IVSMPCRERF EALTETERAA LFPKGVPVVA VEAGVTRGWR GLSGTRADGI IAIGIDRFGE
SAPEKDLWPL FGFTPEAVAD AVRRAVG
