ID   B1XT67_POLNS            Unreviewed;       664 AA.
AC   B1XT67;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   OrderedLocusNames=Pnec_0249 {ECO:0000313|EMBL:ACB43544.1};
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB43544.1};
RN   [1] {ECO:0000313|EMBL:ACB43544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1 {ECO:0000313|EMBL:ACB43544.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT   "Complete sequence of Polynucleobacter necessarius STIR1.";
RL   Submitted (MAR-2008) 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   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; CP001010; ACB43544.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1XT67; -.
DR   STRING; 452638.Pnec_0249; -.
DR   KEGG; pne:Pnec_0249; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_4; -.
DR   OrthoDB; 8732661at2; -.
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          355..526
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   664 AA;  72292 MW;  4B7C931AF8311883 CRC64;
     MSNLQIRMAN AIRALSMDAV QQANSGHPGM PMGMADIAVG LWNEHLKHNP TDPHWIDRDR
     FVLSNGHGSM LLYSLLHLSG YDLPIEELKN FRQLHSKTPG HPEYGITPGV ETTTGPLGQG
     ISNAVGMALA EKLLAEEFNR PGHNIVDHYT YVFLGDGCLM EGISHEVCSL AGILKLNKLI
     ALWDDNGISI DGKVVSWFNE DTPKRFEAYG WNVICDVDGH DAEAVSAAIA KAKKSDKPTL
     ICCKTAIGQG SPNMAGSDKV HGSPLGAAEI AATRVALNWP YPPFEIPKDI YAAWDFKKRG
     QAAEHEWNKE FQKYKNKFPE LASELQRRME GELSKEFSST LSTYLKTCQS KAETIATRKA
     SQNAIEALAP ALPEFMGGSA DLTGSNLTNW STCKAVRGDQ WGNHINYGVR EFGMGAIMNG
     IALHGGYIPF GGTFLTFSDY SRNALRMAAL MKLRSIFVFT HDSIGLGEDG PTHQSVEHVA
     SLRLIPNLMV WRPCDTTESA VAWGSAIGRK NGPSALIFSR QNCPFVSRTP AQIKDIARGG
     YVLRDPKSAK IDAVIIATGS EIALALQTAE HLEKEGLGIR VVSIPSTTVF DQQDAAYKAK
     VLPANIPRVA VEAGVSDFWW KYGCAAAHGV DTFGESAPAL VLYEYFGLTV GQIAKTVKQC
     ISKK
//