ID A1UJ84_MYCSK Unreviewed; 349 AA.
AC A1UJ84;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Transketolase, central region {ECO:0000313|EMBL:ABL92892.1};
GN OrderedLocusNames=Mkms_3698 {ECO:0000313|EMBL:ABL92892.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92892.1};
RN [1] {ECO:0000313|EMBL:ABL92892.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL92892.1};
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP000518; ABL92892.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UJ84; -.
DR STRING; 189918.Mkms_3698; -.
DR KEGG; mkm:Mkms_3698; -.
DR HOGENOM; CLU_012907_1_0_11; -.
DR OrthoDB; 3457658at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-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.
PE 4: Predicted;
FT DOMAIN 27..202
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 349 AA; 38085 MW; 96923F47B5616363 CRC64;
MTQLIERPTG ADDHDRFFTD VPTVTELTMV QAINRALHDA MAADDRVLVF GEDVATLGGV
FRVTDGLSET FGEQRCFDTP LAESAIVGIA IGMAIRGFVP VPEIQFDGFA APAFDQVVSH
LAKYRMRTRG DVDMPVTIRI PSFGGIGAVE HHSESTETYW LHTAGLKVVT PSSPTDAYWL
LRHAIAARDP VIYLEPKRRY WARGAVDTTE PGLPIGRAAV RREGTDVTVL TYGPLVATAL
SAAEHAAAES DWSLEVVDLR SLNPLDFDTV AASVGKTGRA VVMHEGPRTL GFGAELAARI
SEELFYDLEA PVLRATGFDT PYPPARLEKL WLPGVDRLLD CVQRTLEMP
//
