ID A0A077DEB4_9BURK Unreviewed; 672 AA.
AC A0A077DEB4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=IX83_03600 {ECO:0000313|EMBL:AIL32511.1};
OS Basilea psittacipulmonis DSM 24701.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Basilea.
OX NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32511.1, ECO:0000313|Proteomes:UP000028945};
RN [1] {ECO:0000313|EMBL:AIL32511.1, ECO:0000313|Proteomes:UP000028945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32511.1,
RC ECO:0000313|Proteomes:UP000028945};
RX PubMed=24581117; DOI=10.1186/1471-2164-15-169;
RA Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L.,
RA Francois P., Pilo P., Frey J., Schrenzel J.;
RT "A genomic perspective on a new bacterial genus and species from the
RT Alcaligenaceae family, Basilea psittacipulmonis.";
RL BMC Genomics 15:169-169(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; CP009238; AIL32511.1; -; Genomic_DNA.
DR RefSeq; WP_038499235.1; NZ_CP009238.1.
DR AlphaFoldDB; A0A077DEB4; -.
DR STRING; 1072685.IX83_03600; -.
DR KEGG; bpsi:IX83_03600; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_4; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000028945; Chromosome.
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:UP000028945};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AIL32511.1}.
FT DOMAIN 356..535
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 672 AA; 72919 MW; 04AD3071BDAA2B65 CRC64;
MNRISNAIRA LTMDAVQKAK SGHPGAPMGM AEMAQALWTK HLRHHPKNPN WYDRDRFVLS
NGHGSMLLYA LLHLTGYDVS IDDIKDFRQL HSKTPGHPEV GITAGVETTT GPLGQGITNA
VGFALAESLL ALEFNKPGHD IVDHYTYAFV GDGCLMEGVS HEACSLAGAL KLSKLIVLYD
DNGISIDGQV SPWFNDDTPK RFEAYGWNVI RNVDGHDVDA VSDAIEQAKA NAKKPNAGPT
LICCKTVIGK GSPNMSGTSS VHGSPLGEAE IQATREALGW DYAAFEIPED IYQAWSQVER
GQALENEWKV SFARYQSLYP ELAAEFERRM KGELPADFAE KAQAALKAVA EKAETIATRK
ASQNAITALV SILPEMLGGS ADLTGSNLTD WKGAVAVRPG VLGRHINYGV REFGMAAIMN
GIALHGGYLP FGGTFLTFSD YSRNAIRMAA LMKQRVVHVF THDSIGLGED GPTHQSVEHA
ASLRIIPNLD VWRPCDSTET MVAWIQAVSR PESVGMDVKE GGPTALLLSR QNLPFVSRTE
EQLAAIAHGA YVLKETANPK VVLMATGSEV EIALKAQQLL EEEGIGSRVV SMPCTNVFDR
QSRQYQQSIL PKDLPKVAIE AGVTDFWRKY VGIDGAVLGL DRYGESAPAG VLFKHFGLTA
EHLAQTAKEL IH
//
