ID   A0A345RAM2_9RHOB        Unreviewed;       673 AA.
AC   A0A345RAM2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   Name=tkt {ECO:0000313|EMBL:AXI54609.1};
GN   ORFNames=C1J05_08975 {ECO:0000313|EMBL:AXI54609.1};
OS   Sulfitobacter sp. JL08.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=2070369 {ECO:0000313|EMBL:AXI54609.1, ECO:0000313|Proteomes:UP000253748};
RN   [1] {ECO:0000313|EMBL:AXI54609.1, ECO:0000313|Proteomes:UP000253748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL08 {ECO:0000313|EMBL:AXI54609.1,
RC   ECO:0000313|Proteomes:UP000253748};
RA   Pohlner M., Engelen B., Bunk B.;
RT   "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL   Submitted (JAN-2018) 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; CP025815; AXI54609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345RAM2; -.
DR   KEGG; suli:C1J05_08975; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000253748; Chromosome.
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:UP000253748};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          357..528
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   673 AA;  72973 MW;  7DD7D9E354A269AE CRC64;
     MDIAALSAAH PDHWSKATAI RTLTLDAVKA ANSGHSGMPM GMADVATVLF EKHLKFDASA
     PNWPDRDRFI LSAGHGSMLL YSLLYLTGYK DMSLEEIKNF RQWGSRTAGH PEYGHAAGIE
     TTTGPLGQGI SNAVGFAMAE EMQRAHYGRK AVDHFTYVIA GDGCLMEGVS QEAIGLAGRH
     ELSKLIVLWD NNNITIDGTV DIADRTDQVA RFKASGWNVL EIDGHDPVAI DAALTQAKKG
     NKPTMVACKT HIALGHAAQD TSKGHGALTD EDQLAAAKAA YGWKTGPFEI PADVKSAWEA
     IGARGATTRA EWEARFATLP GNKQREFNRA YALDAPKKLS ATIKAFKKQM TESAPKLATR
     ASSEKVLEVI NPIMHETVGG SADLTGSNNT KTADLGVFLP ENRKGRYIHY GIREHGMAAA
     MNGMVLHGGM RPYGGTFMCF TDYARPAIRL AALMRIPTVF VMTHDSIGLG EDGPTHQPVE
     HLAISRATPN TYVFRPADTI ETAEAWEIAL TSKETPSVLS LTRQGLRTVR TEHKTKNMTA
     QGGYVLADAE GKREAILMAT GSEVEIALAA RDLLQAEGIG TRVVSMPCWE LFEDQDERYR
     KRVLPGGPVR VAIEAGIRFG WDRWLFGERG KREKSGFIGM HGFGASAPAD VLYEQFGITA
     EATAAKVKSL LKK
//