ID A0A0M9EID2_9RHOB Unreviewed; 673 AA.
AC A0A0M9EID2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tktA {ECO:0000313|EMBL:KPA22320.1};
GN ORFNames=shim_05980 {ECO:0000313|EMBL:KPA22320.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22320.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA22320.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA22320.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-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}.
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:KPA22320.1}.
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DR EMBL; LAJH01000009; KPA22320.1; -; Genomic_DNA.
DR RefSeq; WP_054001136.1; NZ_LAJH01000009.1.
DR AlphaFoldDB; A0A0M9EID2; -.
DR STRING; 1389006.shim_05980; -.
DR PATRIC; fig|1389006.3.peg.615; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000037951; 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:UP000037951};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPA22320.1}.
FT DOMAIN 357..528
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 673 AA; 71964 MW; 4C093BECF7DEEADB CRC64;
MDIATLKENN PEHWMKAAAI RALTLDAVAA ANSGHSGMPM GMADVATVLF EKHMKFDVAA
PSWPDRDRFI LSAGHGSMLI YSLLYLMGDA QVTLEQVKNF RQMGALTAGH PENFLIDAVE
TTTGPLGQGL ANAVGFAMAE EIQRAQYGRK IVNHNTYVIA GDGCLMEGIS QEAIGLAGRH
SLGNLVVLWD NNNITIDGSV DLSDRTDQVK RFKASGWHVQ EIDGHDPAAI DAAITAAKKA
KKPSMIACKT HIAIGHAAQD TSKGHGALTD ADQMAAAKAA YGWTTGPFEV PSDIKAQWEA
IGTRGAADRA EWEARFADVS KQKQARFNRA YALDVPNKLS ATVKALKKKI SEELPTVATR
KSSEMTLAAI NPIMPETVGG SADLTGSNNT LTADLGVFDT DNRGGRYVYW GIREHGMAAA
MNGMALHGGI RPYGGTFFCF TDYARPSMRL AALSKIPTVF VMTHDSIGVG EDGPTHQPVE
HLAICRATPN TYVFRPADSV ETAEAWEIAL SSKDTPSVMA LTRQNLPTLR TEHKLKNLTA
QGGYVLAEAE GKRQAILIAT GSEVATAMEA KKLLEAEGIG TRVVSMPCME LFAAQDEAYR
RKVLPAGGAV RVGIEAAVRA GGWDQLLLGE RARAGKSDFV GMDRFGASAP AGELFEKFGI
TAANVAEKAK ALL
//
