ID A0A126ZCB0_9BURK Unreviewed; 704 AA.
AC A0A126ZCB0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AMM24779.1};
GN ORFNames=AX767_10765 {ECO:0000313|EMBL:AMM24779.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM24779.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM24779.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM24779.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-2016) 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}.
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DR EMBL; CP014517; AMM24779.1; -; Genomic_DNA.
DR RefSeq; WP_068631186.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZCB0; -.
DR STRING; 1795631.AX767_10765; -.
DR KEGG; vaa:AX767_10765; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000070169; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR033248; Transketolase_C.
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; 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:UP000070169};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 356..563
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 413..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 75336 MW; 0DE9E203622D1FB7 CRC64;
MANQALMANA IRALAMDAVQ QANSGHPGAP MGMADMAVAL WGDHLRFNPA NPHWFDRDRF
VLSNGHASMM LYAVLHLSGY DLPMSEIKNF RQLHSKTPGH PEIDVTPGVE TTTGPLGQGI
TNAVGMALAE KLLAAEFNRK GHEIVDHHTY AFLGDGCMME GISHEAAGLA GAWRLGKLIA
LYDDNGISID GQVKPWFIDN TKERFEAHGW NVIGTIDGND AKDVSKAIAK AKKNSDNKPT
LIICKTVIGK GSPNRAGTAK AHGEALGAEE IKLTREAIGW TEPAFEIPQI VADDWNHQAA
GAKVEAEWNE KFAAYGAAFP DLAAEFTRRM KGELPKNFHQ VAFDTVVAAH TKAETVASRK
ASQLALESFT AALPEMLGGS ADLTGSNLTN TKSTAPFRVD PKTGDVVLGA PHEAAKQGAE
DESKPKSTTD AAPAPHGVIG RHINYGVREF GMAAVMNGVA VHGGYIPYGG TFLTFSDYSR
NAIRMAALMK RRVIHVFTHD SIGLGEDGPT HQSIEHAASL RLIPNLDVWR PGDTAETAVA
WAVALQNQSR PTALLLSRQN IAYAPKTDLS DINKGAYVVS EPEAVGLKSK KTVAVIIATG
SEVQLALAAQ KLLATKKIAV RVVSMPSTTT FDRQDMAYKK AVLPKKLPRV AVEMGCTGGW
WKYGVAAVVG IDTFGESAPA PELFKHFGFT PENVAATVEA VLKG
//
