ID A0A0N7LSF9_9RHOB Unreviewed; 673 AA.
AC A0A0N7LSF9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tktA {ECO:0000313|EMBL:CUH53508.1};
GN ORFNames=SHM7688_02962 {ECO:0000313|EMBL:CUH53508.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH53508.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH53508.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH53508.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYPW01000027; CUH53508.1; -; Genomic_DNA.
DR RefSeq; WP_058240659.1; NZ_FOMU01000002.1.
DR AlphaFoldDB; A0A0N7LSF9; -.
DR STRING; 321267.SHM7688_02962; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000054823; 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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054823};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH53508.1}.
FT DOMAIN 357..528
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 673 AA; 72531 MW; 8EC09347312DF642 CRC64;
MDIAALREKN PEHWMKAAAI RALTLDAVAA ANSGHSGMPM GMADVATVLF EKHMKFDVAA
PNWPDRDRFI LSAGHGSMLI YSLLYLMGDK QLTHEQLVNF RQMGALTAGH PENFLLDAVE
TTTGPLGQGI SNAVGFAMAE EIQRAQYGRK LVDHYTYVIA GDGCLMEGIS QEAIGLAGRH
SLGHLIVLWD NNNITIDGTV ELSDRTDQVK RFKASGWHVL EIDGHDPEAI DAAIEAAKKT
KKPSMIACKT HIAIGHAAQD TSKGHGALTD ADQLAAAKDV YGWTDGAFEV PAEIKAQWEA
IGARGAADRE AWEARFAEAS KQKQDRFNRA YALDVPKKLS ATVKALKKQI SEDKPSVATR
KSSEMALAAI NPIMPETVGG SADLTGSNNT KTGDLGVFDT DNRKGRYVYW GIREHGMAAA
MNGMALHGGI RPYGGTFFCF TDYARPSMRL AALSKIPTVF VMTHDSIGVG EDGPTHQPVE
HLAICRATPN TYVFRPADSV ETAEAWEIAL TSKETPSVMA LTRQNLPTLR TEHKLANLTE
KGAYVLAEAE GKRQVILIAT GSEVSTAMEA KALLEAEGIG TRVVSMPCME LFAQQDEAYR
RKVLPAGAAV RVGVEAAVRA GGWDQWLLGE RARPGKSDFV GMSSFGASAP AGELFEKFGI
TAANVAQKAK DLL
//
