ID A0A1W9KRR8_9BURK Unreviewed; 689 AA.
AC A0A1W9KRR8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=BWK72_14975 {ECO:0000313|EMBL:OQW87038.1};
OS Rhodoferax ferrireducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=192843 {ECO:0000313|EMBL:OQW87038.1, ECO:0000313|Proteomes:UP000192505};
RN [1] {ECO:0000313|EMBL:OQW87038.1, ECO:0000313|Proteomes:UP000192505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7 {ECO:0000313|EMBL:OQW87038.1};
RA Sharrar A.M., Flood B.E., Bailey J.V., Jones D.S., Biddanda B.,
RA Ruberg S.A., Marcus D.N., Dick G.J.;
RT "Novel large sulfur bacteria in the metagenomes of groundwater-fed
RT chemosynthetic microbial mats in the Lake Huron basin.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OQW87038.1}.
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DR EMBL; MTEI01000011; OQW87038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9KRR8; -.
DR Proteomes; UP000192505; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 364..535
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 689 AA; 74008 MW; 416275D7C26DC7A8 CRC64;
MTTPTPEFAK QMANAIRMLA VDAVEKAKSG HPGAPMGMAD IAEVLWNRHL RHNPTNPHWP
DRDRFVLSNG HGSMLIYALL HLTGYDLPMS ELQNFRQLHS KTAGHPEVGV TPGVETTTGP
LGQGITNAVG MALAEKLLST EFNKAEHAIV DHYTYVFLGD GCLMEGISHE ACSLAGTLRL
SKLVAFYDDN GISIDGHVEG WFTDDTPKRF EAYDWNVIPA VDGHNPAAID AAIKAAKAQA
VLPDGKPTLI CCKTVIGMGS PNKAGTHDVH GAALGAAEVA ATREALGWTA APFEIPADIA
TAWNAVARGV SAEHAWDAKF AAYRAAFPTQ AAEFVRRMAG DLPAEFADKL PGLLEGIAAN
ATSFATRKSS QNALDAIAPL LPEFFGGSAD LTGSNLTNFK GCVKAGRDKW GNHMSYGVRE
FGMAAIMNGI TLHGGYIPYG GTFLTFSDYS RNAIRMAALM KIRVIHVFTH DSIGLGEDGP
THQSIEHIPS MRIIPGLDVW RPADGLETAV AWACAVERKD GPSALCLSRQ NLPRLTDVSM
VDNIRKGGYI LSDMENFQAV IVSTGSELEI AMKAQAELAA DGIATRVVSM PSTNVFDRQT
DAYQEMVIPF GTPSLAIEAA HPDFWRKYVG RHGVVIGMPT FGESAPAPKL YAHFGITVER
VVENIRTIVH RAASKRGDSL PDTVVPSIN
//
