ID   B4SPS0_STRM5            Unreviewed;       759 AA.
AC   B4SPS0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Transketolase domain protein {ECO:0000313|EMBL:ACF52340.1};
GN   OrderedLocusNames=Smal_2640 {ECO:0000313|EMBL:ACF52340.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF52340.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF52340.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF52340.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP001111; ACF52340.1; -; Genomic_DNA.
DR   RefSeq; WP_012511587.1; NC_011071.1.
DR   AlphaFoldDB; B4SPS0; -.
DR   STRING; 391008.Smal_2640; -.
DR   KEGG; smt:Smal_2640; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_012907_2_1_6; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 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); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          421..602
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   759 AA;  81993 MW;  65A3DEC532B28463 CRC64;
     MFAVVPDPIP ARMRVLNRAE VCDVNFLDAV RGWRGTPRPR PAPDAPILPG STLTAAAFDD
     LFDSQLASRQ LDLMARVLRV QNKVFYTIGS SGHEGNALLA RACRHTDPAF LHYRSGAFMA
     ERSRQVPGID PLRDAALSFA ASADDPASGG RHKVWGSKPL WVLPQTSTIA SHLPKALGTA
     LAIESGKRLG QPLPIPADSI VLCSFGDASS NHATAQTAFN TAMWSAYQKL PAPILFVCED
     NGLGISVKTP EGWIAERFSH QPGLDYFFAD GLDLAVGHAQ VQAAVEHCRR TRRPTFLHLR
     TTRLMGHAGT DFEVEWRALP ELCAAEAQDP LLRSAQIALE SGWMDAAAIE VAYETMRARC
     MAAAAEAEGR PRLQSLEEVM APLAPYTPAA VQVEAERGPP VDAREALYGG ADALPERQPP
     RHLAIQINHG LQELLAKYPQ SLLFGEDVAQ KGGVYTVSKD LQRRFGPRRV FNTLLDETMI
     LGMAQGLANM GMLPIPEIQY LAYLHNAIDQ LRGEACSLQF FSNDQYRNPM LVRVAGLGYQ
     KGFGGHFHND NSITALRDIP GLVVGCPSRG DDAVMMLRTL AALARVDGRV AVFLEPIALY
     MSKDLHEPGD GQWLFDYPAP GQALVPGEGR VYAPDAGDLV VYTYGNGVPM ALRAARAIEQ
     QLGWQVRVVD LRWLVPLDAG FIAAQAASAR RVLVLDEGRH SGGVGEGVVT ALVEAGFGHL
     PLRRVCGADT YTPLAGAAMF GLPSDNAVIG AALELAQEP
//