ID I3UA32_ADVKW Unreviewed; 324 AA.
AC I3UA32;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AFK61870.1};
GN OrderedLocusNames=TKWG_07195 {ECO:0000313|EMBL:AFK61870.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK61870.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK61870.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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; CP003555; AFK61870.1; -; Genomic_DNA.
DR AlphaFoldDB; I3UA32; -.
DR STRING; 1036672.TKWG_07195; -.
DR KEGG; aka:TKWG_07195; -.
DR HOGENOM; CLU_009227_4_3_4; -.
DR Proteomes; UP000005267; Chromosome.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR049557; Transketolase_CS.
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; PF00456; Transketolase_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..259
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
SQ SEQUENCE 324 AA; 35183 MW; A3A9CD1F1036CF2E CRC64;
MTTTAATSNS HLSNAIRALA MDAVQQANSG HPGAPMGMAE IAEALWTRHL RHNPADPAWA
DRDRFVLSNG HGSMLLYALL HLTGYDLPID ELRQFRQLHS KTPGHPEVGI TPGVETTTGP
LGQGLSNAVG FALAEQLLAA EFNKPEHKIV DHYTYAFVGD GCLMEGISHE VCSLAGTLKL
SKLIVLYDDN GISIDGKVEP WFADDTGKRF EGYGWNVIRG VDGHDVFAVD HAIAKAKQQA
QRGSSGPTII ICKTTIGKAP LIYRVATRFM AHRWARRKLP PRAKPLAGRY RLLKFPKMSM
PAGTSANAVI RFSATGKNSL RSIA
//