ID A0A1H2BVH8_9ACTN Unreviewed; 704 AA.
AC A0A1H2BVH8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN04489716_4936 {ECO:0000313|EMBL:SDT62221.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT62221.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDT62221.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT62221.1,
RC ECO:0000313|Proteomes:UP000198688};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; LT629758; SDT62221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2BVH8; -.
DR STRING; 113562.SAMN04489716_4936; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000198688; Chromosome i.
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; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 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:UP000198688};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 371..551
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 704 AA; 75917 MW; 274E9BE2F3F4F3F8 CRC64;
MAATDPALNW SDLDRKAVDT TRVLAMDAVE KAGNGHPGTA MSLAPAAYLL FNRVLRHDPT
DPEWAGRDRF VLSCGHSSLT LYVQLFLNGY SLSLDDLKSL RQWDSLTPGH PEYGHTPGVE
ITTGPLGQGI GNAVGMAMSA RRERGLLDPD TAAGESPFDH FVYSIASDGD IEEGVSHESS
AIASVQKLGN LVVIYDDNEI SIEDDTRIAK SEDVGKRYEA YGWHVQTVNW RKGETYAEDV
EELWTAIQTA KSVTDKPSFI VLKTIIGFPA PKKQNTGKIH GSALGAAEIT ATKELLGFTD
EPFAIDDEVV KHAQQVVERG RAARAEWQKA FDAWAAGNAE GKVLFDRLAT RTLPEGWLKA
LPVFPADEKG VATRAASGKI LEALAPVLPE LWGGSADLAE SNNTTMKGEP SFIPAEYATE
AFPGHEYGRT LHFGIREHGM GSILNGIAVH GGTRPYGGTF LVFSDYMRGS VRLSALMKLP
VVFVWTHDSI GLGEDGPTHQ PIETLTALRA IVGLDVVRPA DANETAYAWR GALEHDDRPT
ALALSRQNLP TLDRTKYASA EGTLKGGYIL SEASTGTPQV ILVASGSEVS IALTAQERLE
ADGTPTRVVS MPCQEWFYQQ DVAYQQQVLP SGVKARVTVE AGIRMSWDRI LGDAGEAVSI
EHYGASAPAK VLFEQFGFTA DNVVAKAHAS LARVGEITGH KTGN
//
