ID A0A1J7BJV7_9ACTN Unreviewed; 701 AA.
AC A0A1J7BJV7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=BIV57_03160 {ECO:0000313|EMBL:OIV38967.1};
OS Mangrovactinospora gilvigrisea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Mangrovactinospora.
OX NCBI_TaxID=1428644 {ECO:0000313|EMBL:OIV38967.1, ECO:0000313|Proteomes:UP000243342};
RN [1] {ECO:0000313|EMBL:OIV38967.1, ECO:0000313|Proteomes:UP000243342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 26 {ECO:0000313|EMBL:OIV38967.1,
RC ECO:0000313|Proteomes:UP000243342};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces gilvigriseus MUSC 26.";
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}.
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:OIV38967.1}.
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DR EMBL; MLCF01000009; OIV38967.1; -; Genomic_DNA.
DR RefSeq; WP_071655081.1; NZ_MLCF01000009.1.
DR AlphaFoldDB; A0A1J7BJV7; -.
DR STRING; 1428644.BIV57_03160; -.
DR Proteomes; UP000243342; 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; 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:UP000243342};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 373..554
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 701 AA; 75084 MW; 596DEC2FBDB20D04 CRC64;
MSATPTKPND LEWTDLDKQA VDTVRVLAMD AVQKVGNGHP GTAMSLAPAA YLLFQKHLQH
DPADPHWVGR DRFVLSAGHS SLTLYIQLYL SGYGLSLDDL KSFRTWGSLT PGHPEHGHTA
GVEITTGPLG SGIAAATGMG MASRYERGLF DPDTADGESP FDHRIYVIAS DGDLQEGVSG
EAGSLAGHQR LGNLIVIYDD NNISIEGDTE TAFSEDVLGR YEAYGWHTQA VPHLADGDVD
VEGLHRALLA AEEETERPSI IKLSTIIGWP APNKQNTAGA HGSALGADEV AATKRVLGWD
PEQSFQVDDA VLAHARQIGE RGRAAHKAWD GELAKWRADQ PQRAAEFDRI AAGRLPDGWE
KKLPEFPADA KGVATRAASG KVLEALGPVI PELWGGSADL AGSNNTTIDK NSSFEAKGNP
LPGADPYGRT IHFGIREMSM GMALNGIALH GNTRVYGGTF LTFSDYMRGA VRLAALMELP
VTYVWTHDSI GLGEDGPTHQ PVEHMAALRA IPGLNMVRPG DGNETVVAWR EILTRYNDKP
APHGLALTRQ NIPTWDRSGG EFASAEGTAK GGYVLQEATG GTPQVILIGT GSEVQLAVEA
RATLEADGIP TRVVSMPSME WFQEQPEAYR TEVLPTAVKA RVSVEAGIAQ PWYRYLGDAG
RAVSLEHFGA SADYKTLYQE FGITADAVVQ AARESLQAAS A
//
