ID A4XXD3_PSEMY Unreviewed; 334 AA.
AC A4XXD3;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Transketolase, central region {ECO:0000313|EMBL:ABP85999.1};
GN OrderedLocusNames=Pmen_3246 {ECO:0000313|EMBL:ABP85999.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP85999.1};
RN [1] {ECO:0000313|EMBL:ABP85999.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP85999.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP85999.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XXD3; -.
DR STRING; 399739.Pmen_3246; -.
DR KEGG; pmy:Pmen_3246; -.
DR PATRIC; fig|399739.8.peg.3293; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_6; -.
DR OrthoDB; 9780894at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 12..187
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 334 AA; 36159 MW; B7F2C1F319EFF288 CRC64;
MSEKPAPSEK KVSLLEAVNL ALHRAMAEDE NVVVLGEDIG VNGGVFRATA GLRDAFGFKR
VIDTPLAETM IAGLSVGMAA QGLKPVMEIQ FMGFIYPALD HLICHASRLR NRTRGRLSCP
MVLRTPMGAG IRAPEHHSES TEALLAHIPG LRVVIPSSPA RAYGLLLAAI DDPDPVVFLE
PTRLYRMNPQ PLADDGRRLP LDSCFTLREG RDLTLVSWGA SIHETLQAAD RLAERGIAAE
VIDVACVKPL DVDTLEASVR KTGRCVIVHE APKSCAVGAE IAASLYERAL LDLQAPIQRV
TAPDIPPPLY RLEQLYIPGV EDILAACETV LEYA
//
