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Database: UniProt
Entry: M3GSU2_LEPIR
LinkDB: M3GSU2_LEPIR
Original site: M3GSU2_LEPIR 
ID   M3GSU2_LEPIR            Unreviewed;       320 AA.
AC   M3GSU2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Transketolase, pyridine binding domain protein {ECO:0000313|EMBL:EMG09698.1};
GN   ORFNames=LEP1GSC151_2626 {ECO:0000313|EMBL:EMG09698.1};
OS   Leptospira interrogans serovar Grippotyphosa str. LT2186.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1001599 {ECO:0000313|EMBL:EMG09698.1, ECO:0000313|Proteomes:UP000011776};
RN   [1] {ECO:0000313|EMBL:EMG09698.1, ECO:0000313|Proteomes:UP000011776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2186 {ECO:0000313|EMBL:EMG09698.1,
RC   ECO:0000313|Proteomes:UP000011776};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA   Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EMG09698.1}.
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DR   EMBL; AFME02000306; EMG09698.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3GSU2; -.
DR   BioCyc; LINT1001599:G11K9-3319-MONOMER; -.
DR   Proteomes; UP000011776; 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; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
PE   4: Predicted;
FT   DOMAIN          12..177
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   320 AA;  34782 MW;  BE0C2397559237CF CRC64;
     MGAPSTSTAT EKATRDGYGD ALHELGASRP DVVVLDADLS GSTKTNKFAK AFPDRFFNVG
     VAEQNLVGHA AGLALSGLVP FASSFAMFLS GRAWEIVRNS VVYPFLNVKL VASHGGITVG
     EDGASHQCIE DFAIMRVIPE MTVICPSDYN ECKQIIHAIA DYKGPVYVRV GRPNVPIIER
     ENYKFQIGKA EVMREGKDVL IIANGVLVNE AIKASEELSK EGIQVTLLNM ATIKPIDKET
     ILKYAKECGI VVTCEEHNVV GGLGSAVSEF LSEEYPVHVL KVGMKDQFGK SGTWKELLDY
     FGLRSKNIVE TVKKAKTLKK
//
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