ID   A0A0S6X550_9SPHN        Unreviewed;       662 AA.
AC   A0A0S6X550;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=MBENS4_3382 {ECO:0000313|EMBL:GAM06385.1};
OS   Novosphingobium sp. MBES04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM06385.1};
RN   [1] {ECO:0000313|EMBL:GAM06385.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBES04 {ECO:0000313|EMBL:GAM06385.1};
RA   Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA   Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT   "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT   Sunken Wood from Suruga Bay, Japan.";
RL   Genome Announc. 3:e01373-14(2015).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DF850489; GAM06385.1; -; Genomic_DNA.
DR   RefSeq; WP_039392965.1; NZ_DF850489.1.
DR   AlphaFoldDB; A0A0S6X550; -.
DR   STRING; 1206458.MBENS4_3382; -.
DR   HOGENOM; CLU_009227_0_0_5; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000053513; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          349..520
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   662 AA;  70797 MW;  88E611712F5A81C0 CRC64;
     MTLAPARLAP MANAIRALSM DAVQAANSGH PGMPMGMADV ATVLYAKHLK FDPKNPQWAD
     RDRFVLSAGH GSMLMYSLLY LTGYESPTIE DIRNFRQMGS PCAGHPENFL LEGVECTTGP
     LGQGLAMAVG MAMAERQLNA TFGDDLVDHN TWVIAGDGCL MEGINHEAIG LAGTLGLGKL
     KVLWDDNDIT IDGKTGLSTS EDIPARYRAS GWDVFSCDGH DFADIERALA EAAASDKPTL
     VGCKTVIGKG APNKQGGSGV HGSPLGADEI AAAREVLGWS AEPFVIPEDI LADWRSLGAK
     GAEAREAWEA RKVANPEAAE FSRRMAGELP DTEEVAKTFA GWLEGDANVA TRKASENCLN
     VLAPALPEMI GGSADLTGSN NTKAKCQEPF TAENYAGRYV YYGIREFGMA AAMNGMALHG
     GVIPYGGTFL IFSDYCRNAI RLSALQQVRA IYVLTHDSIG LGEDGPTHQP VEQVMSLRLI
     PNLNVFRPAD VIETAECWNI ALQTQETPSV LALTRQNLPQ LRTSGEMLSA RGAYTLRAAE
     GDRKVILIAS GSEVELACTV RDELQAQGIG ADVVSMPCME LFDAQEEAYK HEVLPHDPSI
     LKVSIEAGTT MGWERYTATS RNGGLNIGLD RFGASAPAQD LFARFGFSAA SIVPKVLEKL
     SV
//