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Database: UniProt
Entry: A0A2I0CST9_9PSED
LinkDB: A0A2I0CST9_9PSED
Original site: A0A2I0CST9_9PSED 
ID   A0A2I0CST9_9PSED        Unreviewed;       329 AA.
AC   A0A2I0CST9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Alpha-ketoacid dehydrogenase subunit beta {ECO:0000313|EMBL:PKF72113.1};
GN   ORFNames=CW360_04770 {ECO:0000313|EMBL:PKF72113.1};
OS   Pseudomonas pharmacofabricae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1905276 {ECO:0000313|EMBL:PKF72113.1, ECO:0000313|Proteomes:UP000242861};
RN   [1] {ECO:0000313|Proteomes:UP000242861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZYSR67-Z {ECO:0000313|Proteomes:UP000242861};
RA   Yu X.-Y.;
RL   Submitted (DEC-2017) 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:PKF72113.1}.
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DR   EMBL; PIYS01000005; PKF72113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0CST9; -.
DR   Proteomes; UP000242861; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000242861};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          7..182
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   329 AA;  35695 MW;  A3F61B7A03087BDE CRC64;
     MNDTTRYSLL EAVNLALHRA MRDDPDVLVL GEDVGVNGGV FRATAGLREA FGARRVIDSP
     LAETMLAGVA VGMAAQGLRP VLEIQFLGFI YAAMEHLISH ASRLRNRTRG RLSCPLVVRS
     PMGAGIRAPE HHSEAVEALF AHIPGLRVVV PSSPARAYGL LLAAIDDPDP VLFLEPTRLY
     RMNPQPLSDD GRRLPLDSCF TLREGSDLTL LSWGASIHEC LQASRQLAEQ GVSVELLDVA
     CLKPLDMASL EASVRKTGRC LIVQEAPQSA GLGAEIAASL YERCFLDLQA PIQRLAAADI
     PPPLYRLEPL YMHSVADIVT ACRQLLDQP
//
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