TKT_RHOCB
ID TKT_RHOCB Reviewed; 672 AA.
AC D5AV94; O68024; Q52723;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tktA; Synonyms=tkt2; OrderedLocusNames=RCAP_rcc02146;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT SB1003.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
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+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AF010496; AAC16110.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85876.1; -; Genomic_DNA.
DR PIR; T03457; T03457.
DR RefSeq; WP_013067855.1; NC_014034.1.
DR AlphaFoldDB; D5AV94; -.
DR SMR; D5AV94; -.
DR STRING; 272942.RCAP_rcc02146; -.
DR EnsemblBacteria; ADE85876; ADE85876; RCAP_rcc02146.
DR GeneID; 31490996; -.
DR KEGG; rcp:RCAP_rcc02146; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_5; -.
DR OMA; NSGHSGM; -.
DR OrthoDB; 188169at2; -.
DR UniPathway; UPA00115; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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; IPR020826; Transketolase_BS.
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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..672
FT /note="Transketolase"
FT /id="PRO_0000410703"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 124..126
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 35
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 266
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 672 AA; 72436 MW; B6B1E7DE1E66CA80 CRC64;
MDLAALRAKT PDHWKLATAI RVLAIDAVQA ANSGHPGMPM GMADVATVLF RNHLKFDAKA
PNWADRDRFV LSAGHGSMLL YALLHLTGYE QATLDEVKNF RQWGARMAGH PEYGHLEGVE
TTTGPLGQGI STAVGMAIAE KSMAARFGKK LVDHKIWVIA GDGCLMEGIS QEAIGLAGKQ
ELDNLIVLWD NNNITIDGRV TVSDVTDQKA RFAASGWDVL SCDGHDAEDI DRALTAAKKA
KRPVLVDCKT LIGFGSPNKA DSYAVHGAPL GDAEIKLTRE AYGWEHGPFV IPAEIKAEWE
AIGAKGAAER AEWEARLAAL PAGKRAEFER QMARGVAPKL AGAIRAFKKA QSEAAPKVAT
RKASEMVLAA VNPVVPETIG GSADLTGSNL TKTSDIEDFM PGNHKGRYMR YGIREHAMAA
AMNGMWLHGG VRPYGGTFFC FTDYARGAMR LSSLMGVPTV YVMTHDSIGL GEDGPTHQPV
EHLAICRATP NTWTFRPADV IETAEAWELA LSSERTPSVL ALSRQNLPTL RTKHEAKNLT
AKGAYVIAEA EGKRQAILMA TGSEVEIALK ARALLQAEAI GTRVVSMPCM ELFAAQDEAY
RKRILPAGGV RVAVEAAIRQ PWDRWLLGER GMERKAGFVG MEGFGASAPA ERLYAEFGIT
PEAIAAKVKS LL
