ID E4M7X1_9BACT Unreviewed; 426 AA.
AC E4M7X1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Transketolase, pyridine binding domain protein {ECO:0000313|EMBL:EFR58958.1};
DE Flags: Fragment;
GN ORFNames=HMPREF9720_1135 {ECO:0000313|EMBL:EFR58958.1};
OS Alistipes sp. HGB5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=908612 {ECO:0000313|EMBL:EFR58958.1, ECO:0000313|Proteomes:UP000002960};
RN [1] {ECO:0000313|EMBL:EFR58958.1, ECO:0000313|Proteomes:UP000002960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB5 {ECO:0000313|EMBL:EFR58958.1,
RC ECO:0000313|Proteomes:UP000002960};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EFR58958.1}.
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DR EMBL; AENZ01000008; EFR58958.1; -; Genomic_DNA.
DR AlphaFoldDB; E4M7X1; -.
DR PATRIC; fig|908612.3.peg.232; -.
DR eggNOG; COG0021; Bacteria.
DR Proteomes; UP000002960; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
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; IPR033247; Transketolase_fam.
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 SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 4: Predicted;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 103..284
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFR58958.1"
SQ SEQUENCE 426 AA; 46162 MW; 1FEA049D5048FC82 CRC64;
PAGESFEDKV STHGQPLTAA GADFAATVKN LGGDPNDPFA VFSESREAFS ERREALRAWA
SRQAEVEKTW RAEHGDLARK LDMFLSGRLP EIDYKSIEVK AGVATRAASA AVLGVFAETI
ENMIVASADL SNSDKTDGFL KKTKAFTKGD FSGKFFQAGV SELTMACVAN GMALHGGVIP
ACGTFFVFSD YMKPAVRLSA LMRLHVIYIW THDSFRVGED GPTHQPIEHE AQIRLMEHLR
NHHDERSMVV LRPADGDETV MAWKLAVEEQ RPVALVLSRQ NIKSLPALGA SRREEAAQVA
KGGYVVLDSA KPEVVMVATG SEVSTLVEGA ELLAAEGIAV RVVNVPSEGL FRDQPRSYQE
SVLPVGVVRY GLTSGLPVNL MGLVGEKGMI HGLDHFGYSA PYTVLDEKFG YNGKTVAEEV
KKLLGK
//
