ID A0A257F0C1_9RHOB Unreviewed; 671 AA.
AC A0A257F0C1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:OYU18750.1};
GN ORFNames=CFE34_08795 {ECO:0000313|EMBL:OYU18750.1};
OS Rhodobacteraceae bacterium PARR1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2015578 {ECO:0000313|EMBL:OYU18750.1, ECO:0000313|Proteomes:UP000216502};
RN [1] {ECO:0000313|EMBL:OYU18750.1, ECO:0000313|Proteomes:UP000216502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PARR1 {ECO:0000313|EMBL:OYU18750.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU18750.1}.
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DR EMBL; NKIT01000045; OYU18750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257F0C1; -.
DR Proteomes; UP000216502; 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:UP000216502};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 357..529
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 671 AA; 71553 MW; 3623097C98221500 CRC64;
MDIETLRARH PDHWMRACAI RTLTLDAVAA ANSGHSGMPM GMADVATVLF EKHLNFDPTA
PRWANRDRFI LSAGHGSMLI YSLLYLTGYA DVTLEQIKNF RQWGAITAGH PEYGHVAGVE
TTTGPLGQGI ANSVGFAIAE ENLRARWGSK IMDHYTYVIA GDGCLMEGVS QEAIGLAGKQ
KLSRLIVLWD DNGITIDGKV SIADVTDQKA RFAASGWNVL SCDGHDPEDI DRALTAAKAS
DRPTMIACKT HIALGHAAQD TSKGHGALTD AAQMAAAKAG YGWTAAPFEI PADIKAQWEA
MGARGAAARA AWEGRLAALS PAKQAEFARI FAGDAPAKLA SVIRGVKKAA VEALPKLATR
SSSEKVLAAV NPVMGETLGG SADLTGSNNT KTADLGVFTP EDRKGRYVYF GIREHGMAAA
MNGMALHGGV RPYGGTFMCF TDYARPSMRL SALMGIPVVY VMTHDSIGLG EDGPTHQPVE
HLAISRSTPN TLVIRPADLV ETAEAWEIAL TQKTTPTVLA LSRQNLPAVR KTHTNTNMVA
KGAYVLAESV AKRQVILIAT GSEVEIALKA KDALEAEGIG TRVVSMPSME LFAQQDEAYR
RKVLPPGPAR VAIEAGVRQG WDRWLLGERG REAKAGFVGM SSFGASAPID RLYKEFGITA
ENTVAVAKSL I
//
