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Database: UniProt
Entry: U2V1T1_9ACTN
LinkDB: U2V1T1_9ACTN
Original site: U2V1T1_9ACTN 
ID   U2V1T1_9ACTN            Unreviewed;       572 AA.
AC   U2V1T1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Transketolase, thiamine pyrophosphate-binding domain protein {ECO:0000313|EMBL:ERL09297.1};
GN   ORFNames=HMPREF1316_1852 {ECO:0000313|EMBL:ERL09297.1};
OS   Olsenella profusa F0195.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=1125712 {ECO:0000313|EMBL:ERL09297.1, ECO:0000313|Proteomes:UP000016638};
RN   [1] {ECO:0000313|EMBL:ERL09297.1, ECO:0000313|Proteomes:UP000016638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0195 {ECO:0000313|EMBL:ERL09297.1,
RC   ECO:0000313|Proteomes:UP000016638};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERL09297.1}.
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DR   EMBL; AWEZ01000030; ERL09297.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2V1T1; -.
DR   STRING; 1125712.HMPREF1316_1852; -.
DR   PATRIC; fig|1125712.3.peg.794; -.
DR   eggNOG; COG2188; Bacteria.
DR   eggNOG; COG3959; Bacteria.
DR   Proteomes; UP000016638; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.1410.10; Chorismate lyase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005474; Transketolase_N.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR011663; UTRA.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   Pfam; PF00392; GntR; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   Pfam; PF07702; UTRA; 1.
DR   PRINTS; PR00035; HTHGNTR.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SMART; SM00866; UTRA; 1.
DR   SUPFAM; SSF64288; Chorismate lyase-like; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016638}.
FT   DOMAIN          39..107
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
SQ   SEQUENCE   572 AA;  61713 MW;  EAB229E938E5D207 CRC64;
     MIWIGQRDGW AMTGDRARFP TPETLDATRG QVDELGQSGP LHARLASLLR QKIVDREWPS
     GMALPSEAEL MEQFCMSRGT VRRALSSLVQ DGYIVTRKGS GSFVAEGGLP RPATRRPLSF
     AALFRERGLR FTTRVLSQSV MGAPRNVAIH LGVGEGSPVL FLRRIRSVGA RPLVCQESWE
     SLRPCPGLER ADFTEESLFD AVERTSGRHI GSSVVHYSSQ RVGRAHAPLL ASEPESSTLV
     LEQDICLTDG TPIEWSVTWM RPGTPVVGVS VEGPVREAAP SVGADGAEGG AGAAALRREL
     DLRALEIRRG VLEIAHRYPH MPFHLGGALS MAEVVAVLLG HVMHTGADGT PWERRDRLVV
     SKAHASVALY PALLRAGIIS QDDLDRGLFG PDAVLFKHPH RDPGRGIELS GGSLGMGLGY
     ACGLALALRR RQLPARVFCI VGDGECDEGS VWESAAFAGH QRLSNLTVVV DANGMQLDGP
     TAQVLDNGPL RRKFEAFGFA VAETDGHDVL ALARALAAPH EGPLAVVART VKGRGLSRAE
     NNVAWHDIAL AQDDYERARV ELGQREEAIR HG
//
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