ID L0DSQ9_THIND Unreviewed; 650 AA.
AC L0DSQ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tktA [H] {ECO:0000313|EMBL:AGA32048.1};
GN OrderedLocusNames=TVNIR_0340 {ECO:0000313|EMBL:AGA32048.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA32048.1, ECO:0000313|Proteomes:UP000010809};
RN [1] {ECO:0000313|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC {ECO:0000313|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) 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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CP003989; AGA32048.1; -; Genomic_DNA.
DR AlphaFoldDB; L0DSQ9; -.
DR STRING; 1255043.TVNIR_0340; -.
DR KEGG; tni:TVNIR_0340; -.
DR PATRIC; fig|1255043.3.peg.340; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_6; -.
DR Proteomes; UP000010809; 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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGA32048.1}.
FT DOMAIN 340..512
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 650 AA; 69810 MW; 45CFCC811A07BDB9 CRC64;
MDAVQKANSG HPGAPMGMAD IAEVLWNDYL KHNPANPGWL DRDRFVMSNG HGSMLVYSLL
HLTGYDLPMS ELQQFRQLHS KTPGHPEYGY TAGVETTTGP LGQGLTNAVG MALAERALAA
HFNRDGHDIV DHHTYVFLGD GCLMEGISHE ACALAGTLGL GKLIAFYDDN GISIDGEVDG
WFTDDTPKRF EAYGWHVARD VDGHSADAVK AAIEQARAET GKPTLICCKT VIGFGSPNKQ
GKEECHGAPL GSDEIELARK ELGWHHAPFE IPAEIQAAWN AREQGAKAEA GWGERFEAYR
AAHPDLAVEL ERRMRGELPA DWAGSAAAFV QQTVEKAEKV ASRKASQNAI AGYAPALPEL
LGGSADLAGS NLTLHPGSKG ISREDPAGNY VFYGVREFGM AAIMNGIALH GGFIPYGGTF
LIFSDYARNG IRMSALMKQR VLYVLTHDSI GLGEDGPTHQ PVEQTPSLRL IPNLNVWRPC
DAVETAVAWK SGIERNDGPS AFILSRQGLA PQQRDGEQVA AIARGGYVLR DCEGTPELIL
IATGSEVAIA AAAAEKLAGE GRRVRLVSMP CVELFEQQDP AYREAVLPAE VRARVAVEAG
ATVGWYKFVG LDGAVIGLDR FGESAPGDAL MEYFGFTADN VAQVARDILN
//
