ID A0A3N2MXJ4_9BACT Unreviewed; 676 AA.
AC A0A3N2MXJ4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:ROT14893.1};
GN ORFNames=EEL48_05235 {ECO:0000313|EMBL:ROT14893.1};
OS Muribaculaceae bacterium Isolate-102 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486470 {ECO:0000313|EMBL:ROT14893.1, ECO:0000313|Proteomes:UP000272558};
RN [1] {ECO:0000313|EMBL:ROT14893.1, ECO:0000313|Proteomes:UP000272558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-102 (HZI) {ECO:0000313|Proteomes:UP000272558};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-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 -!- 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:ROT14893.1}.
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DR EMBL; RIBI01000002; ROT14893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2MXJ4; -.
DR Proteomes; UP000272558; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000272558};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 352..534
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 97..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 72829 MW; ACBCE3DC7C404369 CRC64;
MDKNVLNRAA DNIRVLAASM VEKAKSGHPG GAMGGADFVN VLYSSFLVTD PDNPTWIARD
RFFLDPGHMS SMLYAVLALT GKYTVDELKE FRQWGSVTPG HPEVHPERGV ENTSGPLGQG
HVMAVGSAIA ERFLQARFGD WIAHKTYAFI SDGGIQEEIS QGAGRLAGYL GLNNLIMFYD
SNDIQLSTEV KAVTAEDTAA KYRAWNWNVI EVDGTDPLAM AGALETAIEE KHRPTIIIGK
TVMGRGAVTA EGESYEGKCS THGNPLSKSG ASYEKTMEHL GADPKDPWHI WEDTKKLYAD
RAEVLRATVK LRHEEEKAWR AANPEQAALL DSYIAGKLPE IDWKAIAHKP NIATRQASAD
VLGELAKKVG NMIVASADLA NSDKTDGFLK NTHALTHGDF SGAFLQAGVA ELTMAAIMNG
IALHGGCIAA CGTFFVFSDY MKPAVRMAAL MELPVKYIWT HDAFRVGEDG PTHEPVEQEA
QIRLMEELRN FKGEPSMLVL RPGDAAETSV CWKMAMENTK TPTALILSRQ DIPDLPAASG
DRYNEALGAE KGGYVVVDAA NPDVTLVANG SEVSLLVEVA KLLGAEGVTA RVVSVPSIGL
FEVQPQDYRD SVIPANGKVF GLTAGLPSTL RGVVGRNGEV FGLDHFGASA PYKVLDEKFG
FTAPAVLAQV KAYLAK
//
