ID A0A199AXV8_9ACTN Unreviewed; 703 AA.
AC A0A199AXV8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=AYO52_15135 {ECO:0000313|EMBL:OAV77852.1};
OS Dietzia sp. 111N12-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=1785156 {ECO:0000313|EMBL:OAV77852.1, ECO:0000313|Proteomes:UP000092558};
RN [1] {ECO:0000313|EMBL:OAV77852.1, ECO:0000313|Proteomes:UP000092558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=111N12-1 {ECO:0000313|EMBL:OAV77852.1,
RC ECO:0000313|Proteomes:UP000092558};
RA Yu M.;
RT "Draft genome sequence of Dietzia sp.111N12-1 isolated from South China Sea
RT with petroleum hydrocarbons degradation activity.";
RL Submitted (FEB-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:OAV77852.1}.
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DR EMBL; LSSV01000035; OAV77852.1; -; Genomic_DNA.
DR RefSeq; WP_067716333.1; NZ_LSSV01000035.1.
DR AlphaFoldDB; A0A199AXV8; -.
DR STRING; 1785156.AYO52_15135; -.
DR Proteomes; UP000092558; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..555
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 703 AA; 75013 MW; A7AA165FFC8884B2 CRC64;
MTSASEITEL TTARHPSDWT ELDTRAVDTA RVLAAEAVQR CGSGHPGTAM SLAPLAYTLY
QRIMRHDPSD PTWVGRDRFV LSCGHTSLTQ YIQLYLAGFG LELDDLKALR TWGSKTPGHP
EWRHTDGVEI TTGPLGQGLA SAVGMAMAAR YERGLFDPET PSGKSPFDHF IYVIASDGDV
QEGVTAEASS LAGTQQLGNL IAIYDDNEIS IEDNTRIALN EDVAARYEAY GWHVQTVNGG
EDVAAIEEAI ADARAVTDKP SLIVLRTVIA FPAPTMMNTG ASHGAALGQD EVDAVKEALG
MGGTEPFTVE DEVISHTRAA RDRGARVHAQ WSDMFHAWAE ANPERKTLFD RLYSGELPDG
WDAGLPTWDA DSKGVATRKA SAEAIQALGA TLPELWGGSA DLAGSNNTPI KGADSFGPSS
ISTDTWTASP YGRNLHFGVR EHAMGAILNG IALHGPTRPY GGTFLIFSEY MRPAVRLAAL
QGSNAYYVWT HDSIGLGEDG PTHQPVEQLA ALRAIPGLAI LRPADANETA ASWRAMLEAL
DGPKGLCLTR QDVPVLEGTK ELAREGVERG GYVLAEASTG TPEVILMGTG SEVQLAVQAR
EVLEAEGVAT RVVSMPCVEF FDQQDAGYRE SVLPRSVRAR VSVEAGIAMP WHRFLGDAGR
AVSLEHFGAS APYQTLFTEF GITADAVVSA ARESLAAAAG EAS
//
