ID A0A068YWK5_9BURK Unreviewed; 685 AA.
AC A0A068YWK5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
OS Polaromonas sp. CG9_12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS52939.1, ECO:0000313|Proteomes:UP000043372};
RN [1] {ECO:0000313|EMBL:CDS52939.1, ECO:0000313|Proteomes:UP000043372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Smith H.J., Foreman C.M., Ramaraj T.;
RT "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 2:1-2(2014).
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CCJP01000005; CDS52939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YWK5; -.
DR STRING; 1504672.gene:199032173; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000043372; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDS52939.1}.
FT DOMAIN 359..544
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 685 AA; 73391 MW; DBD8A860F36FC5F1 CRC64;
MAKNEMMANA IRALAMDAVQ QANSGHPGAP MGMADMAVAL WGDHLRHNPA NPHWTNRDRF
VLSNGHASML IYSVLHLTGY QLPIDELKNF RQLHSKTPGH PEVDVTPGIE TTTGPLGQGL
TNAVGMALAE KLLAKEFNRS NGKTDLTIVD HHTYVFLGDG CLMEGISHEA IALAGAWRLN
KLIALYDDNG ISIDGQVAPW FIDNTPMRFA ACGWNVIDAV DGHDAAAVSA AIAGARSSTD
KPTLIVCKTH IGKGSPNRAN TAKAHGEPLG AEEIGLTRTA INWPHTAFDL PKETYAAWDA
KVKGGKHEAA WDKKFAAYTK AHPELAAEFL RRMQGELPKS FSQLAVDTVV GAHTRAETVA
SRKASQLALE SFTAGLPELL GGSADLTGSN LTNTKATPSL RFDANGDVVQ VEAANGSLVG
GRHINYGVRE FGMAAIMNGV ALHGGFIPYG GTFLTFSDYS RNAIRMAALM KLRVVHVFTH
DSIGLGEDGP THQSIEHAAS LRLIPNLDVW RPGDTAETAV AWAVALENKT RPTALLLSRQ
NLPYAPKDDV GQISKGAYVL AEPAEVGLKK KAQAVIIATG SEVQLALKAQ ELLATQKIAV
RVVSMPSTTT FDRQDAAYKS KILPEGIPRI AVEMGVTDGW WKYGCAAVIG IDTFGESAPA
GVLFKHFGFT PENVVATVRK VLRKK
//
