ID A0A0S8CJY7_9CHLR Unreviewed; 673 AA.
AC A0A0S8CJY7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KPK24293.1};
GN ORFNames=AMJ70_02280 {ECO:0000313|EMBL:KPK24293.1};
OS Dehalococcoidia bacterium SG8_51_3.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703394 {ECO:0000313|EMBL:KPK24293.1, ECO:0000313|Proteomes:UP000051285};
RN [1] {ECO:0000313|EMBL:KPK24293.1, ECO:0000313|Proteomes:UP000051285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_51_3 {ECO:0000313|EMBL:KPK24293.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KPK24293.1}.
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DR EMBL; LJTX01000029; KPK24293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CJY7; -.
DR PATRIC; fig|1703394.3.peg.1733; -.
DR Proteomes; UP000051285; Unassembled WGS sequence.
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; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
FT DOMAIN 332..500
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 673 AA; 74054 MW; DB6950CA3A21D17B CRC64;
MSLMNSKIGK TYKNYSVEEL EAAAKLMRGY SLVALGAAGS GHSGGTLSLM DVAAALYLYE
ANLDPKNPFW PDRDRIFWSA GHKAPILYVS LGMAGFFNID EVVTLRKLHS PFQGHPHWLK
LEGIESSSGS LGQGLSISVG DALAARLDKK NYRVYCLMGD GEQQEGQIWE AAMEAGHYKL
DNLCGVVDKN RLQIDGSVDD VMSVDPLADK YRAFGWHVIE IDGHDMKAIL GAFKEARETR
GKPSLIIAHT TKGRGVDFME DVCGWHGKAP SIEQMWNALK QLGLDKKLPV EKLLEKASDY
QAKVTRELEA KQPKFSQNYF WNTTEKMKTE MVPTRMGFGN ALAEHGDDPR VVCLGADISD
SITISQFYKE HPHRSERWLS VGIAEQSGTC VAAGLAKEGK LPVFGTYGVF ASGRNLDQLR
TTVCYGNFNV MIAGAHGGVS VGPDGATHQA LEELFQMCGL PNMHVEVPCD SVETKRATEY
MLFNVVGPKY IRFAREATPV VTDNSTPYKW GEANVIRFRG EKDAFKDAFE HRLASEYKDE
GEDVAIIACG PSVVEAMRAA WILKQEYNLE TRVINMHTVK PLDEKAIAQA AKDCRVVVTA
EEHQVGGLGN LVAAAIGRSE KVYGTPVIMG MIGVQDRFGD SGSPWELVKE FEVSAEHIAA
KAKRLHDLKP SRG
//
