ID A0A0N1MSL0_9SPHN Unreviewed; 662 AA.
AC A0A0N1MSL0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ADT71_25195 {ECO:0000313|EMBL:KPH58656.1}, EDF59_10268
GN {ECO:0000313|EMBL:TCM42106.1};
OS Novosphingobium sp. ST904.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH58656.1, ECO:0000313|Proteomes:UP000037878};
RN [1] {ECO:0000313|EMBL:KPH58656.1, ECO:0000313|Proteomes:UP000037878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:KPH58656.1,
RC ECO:0000313|Proteomes:UP000037878};
RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA Vangronsveld J.;
RT "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT stimulates plant growth.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TCM42106.1, ECO:0000313|Proteomes:UP000295740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:TCM42106.1,
RC ECO:0000313|Proteomes:UP000295740};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (MAR-2019) 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 -!- 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:KPH58656.1}.
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DR EMBL; LGJH01000164; KPH58656.1; -; Genomic_DNA.
DR EMBL; SLVC01000002; TCM42106.1; -; Genomic_DNA.
DR RefSeq; WP_054441415.1; NZ_SLVC01000002.1.
DR AlphaFoldDB; A0A0N1MSL0; -.
DR STRING; 1684385.ADT71_25195; -.
DR PATRIC; fig|1684385.3.peg.3312; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000037878; Unassembled WGS sequence.
DR Proteomes; UP000295740; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037878};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPH58656.1}.
FT DOMAIN 349..520
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 662 AA; 71032 MW; DBAB2F6886D49BA3 CRC64;
MTLAADRLAP MANAIRALSM DAVQAANSGH PGMPMGMADV ATVLFAKFLK FDPAAPKWAD
RDRFVLSAGH GSMLIYSLLH LTGYASPTMD DIRGFRQLGS VCAGHPENFL IEGVECTTGP
LGQGLAMAVG MAMAERQLNA TFGDDLVDHK TWVIAGDGCL MEGINHEAIG LAGTLKLGRL
KVLWDDNKIT IDGDTSLSTS EDIPARYRAS GWDVFECDGH DFADIERALA EAAASDKPTL
VACKTVIGKG APNKQGGHDV HGAALGEAEV AAAREYLGWT SAPFEVPAEI LADWRSLGQA
GATAHADWFG RLAASDKADE FTRRMAGELP ETDAIRAKLA EWLEGDSTVA TRKASENWLN
VLAPAIPEMI GGSADLTGSN NTKAKCQEPF TPDNYGGRYV YYGIREFGMA AALNGMALHG
GVIPYGGTFL IFSDYCRNAI RLSALQQTRA IYVLTHDSIG LGEDGPTHQP VEHVMSMRMI
PNLYVFRPAD VIETAECWNI ALESQDTPSV LALTRQNLPQ LRKTGDMLSA RGAYTLRHAE
GDRKVILIAT GSEVELAVKV KAELESQGIG ADVVSMPCME LFAAQDEAYQ HEVLPNDPSI
LKVSIEAGVT MGWERYTAQS RNGGLNIGLD RFGASAPAKD LFARFGFTVD AIVPKILNKL
SV
//
