ID K0YVS0_9ACTO Unreviewed; 691 AA.
AC K0YVS0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=HMPREF9240_00256 {ECO:0000313|EMBL:EJZ87997.1};
OS Winkia neuii BV029A5.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Winkia.
OX NCBI_TaxID=888439 {ECO:0000313|EMBL:EJZ87997.1, ECO:0000313|Proteomes:UP000006075};
RN [1] {ECO:0000313|EMBL:EJZ87997.1, ECO:0000313|Proteomes:UP000006075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVS029A5 {ECO:0000313|EMBL:EJZ87997.1,
RC ECO:0000313|Proteomes:UP000006075};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces neuii subsp. anitratus BVS029A5.";
RL Submitted (JUL-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=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}.
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:EJZ87997.1}.
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DR EMBL; AGWP01000002; EJZ87997.1; -; Genomic_DNA.
DR RefSeq; WP_004805055.1; NZ_JH815213.1.
DR AlphaFoldDB; K0YVS0; -.
DR PATRIC; fig|888439.3.peg.260; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_11; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000006075; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000006075};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 368..547
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 691 AA; 74944 MW; 79A7A9646A7061C8 CRC64;
MTVKWDDLDK RAVTTAKVLA ADAVEEAGSG HPGTAISLAP LAYLLFQRHL NFDPKDERWL
GRDRFMLSIG HASLIQYIQL YLAGMDMELE DLKQFRKFES KTPGHPEYSH TKGVEITTGP
LGSGFAAAVG FAMSQRRTRG MYDPDAPEGT SPFDHHVYTI VGEGCLEEGI TSEAASLAGT
QGLGNLIVFY DQNLISIEDD TSIAFSEDVP ARFQAYGWHT QQVNFLKDDG SYDEDVNALD
AAIEEAKKVT DRPSLISVRT IIGWPTPGKQ NTGEIHGSAL GEEALVGLKK ALGLDPQKHF
DVDVEAVEHA RANAADRAKQ ARADWDERFA KWQKANPELA AQLSRTLERK LPEGLEEALP
KFEEGKSLAT RAASGKVINA LAPLVPELWG GSADLAGSNK TMMDGEPSFF PQERSSEKFK
GNKYGRNLHF GIREHGMGGI LNGIAADELT RPYGGTFFVF ADYMRGAVRL AALMNLPVTY
VWTHDSIGVG EDGPTHQPVE HLTAYRAIPN LSIVRPMDGP ETGYAWLEVL RRDAPAGLIL
TRQGLPTLHR GEDGLASAAN VAKGAYILKD TEGAPDVLLM GSGSEVQLAV EAAEELAKQG
VAARVISVPC MEWFDQQDDA YKEQVMPAAV TARVSVEAGL PDPWYKYLGC KGKAVAMDSF
GLPGAAGELF EHFGFTAAAV VAKAKEVLSN K
//
