ID   T0I6W5_9SPHN            Unreviewed;       473 AA.
AC   T0I6W5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Transketolase signature 1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L485_02795 {ECO:0000313|EMBL:EQB05344.1};
OS   Sphingobium baderi LL03.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB05344.1, ECO:0000313|Proteomes:UP000015524};
RN   [1] {ECO:0000313|EMBL:EQB05344.1, ECO:0000313|Proteomes:UP000015524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL03 {ECO:0000313|EMBL:EQB05344.1,
RC   ECO:0000313|Proteomes:UP000015524};
RX   PubMed=24051322;
RA   Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT   Sphingobium baderi Strain LL03T.";
RL   Genome Announc. 1:e00751-13(2013).
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EQB05344.1}.
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DR   EMBL; ATIB01000026; EQB05344.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0I6W5; -.
DR   PATRIC; fig|1114964.3.peg.526; -.
DR   eggNOG; COG0021; Bacteria.
DR   Proteomes; UP000015524; Unassembled WGS sequence.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015524}.
FT   DOMAIN          17..361
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          377..456
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02779"
FT   REGION          120..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  50550 MW;  6DBEC7CFD50801A0 CRC64;
     MSTIPASTLH GDGSPERLAI DTIRTLSMDA VHAAKSGHIG TPMALAPVGY TLWSQFLRTD
     PDAPDWPNRD RFVLSVGHAS MLLYSLLHLA AVKEIDKDGR LTGKPAVSLQ DIKDFRQIGS
     KTPGHPEYRH TTGVETTTGP LGQGCGNSVG MAIAERWLAA RYNRDGFPIF DHDVYCLAGD
     GCMMEGVASE AASLAGHLKL SNLCWIYDSN HVTIEGGTDL AFDEDVGQRF DAYGWHVIHV
     DDANDTKAIA AAIESFKATD DKPTLIVVHS IIGYGSSIAG TAKAHGEAMT GDDIRGTKKA
     YGWPEDSSFL VPAGVPEHFE GAIAGRGKPL RAEWLAMRER YAQAEPALAK ELEAIFADRL
     PDGWDAAIPT FPADEKGIAT RDAGGKVLNA IAPNLPWLVG GSADLAPSTK TLIEGAGSFQ
     ASNYAGRNLH FGVREHAMGS VVNGMALSHL RSYSAQSARS CDFGQVEERT LNA
//