ID A0A255EF37_9ACTN Unreviewed; 326 AA.
AC A0A255EF37;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Alpha-ketoacid dehydrogenase subunit beta {ECO:0000313|EMBL:OYN90159.1};
GN ORFNames=CGZ91_08250 {ECO:0000313|EMBL:OYN90159.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN90159.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|EMBL:OYN90159.1, ECO:0000313|Proteomes:UP000216300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN90159.1,
RC ECO:0000313|Proteomes:UP000216300};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-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:OYN90159.1}.
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DR EMBL; NMVJ01000007; OYN90159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255EF37; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000216300; Unassembled WGS sequence.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000216300}.
FT DOMAIN 6..181
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35480 MW; CDED02EADFF5C72D CRC64;
MSVTTMTLGK AINAGLRRAL EADPKVLLAG EDIGKLGGVF RITEGLQKDF GEDRVVDSPL
AESGIVGTAI GMALRGYRPV CEIQFDGFVF PAFNQITTQL SRMYGRTHGR TPMPVVIRIP
TGGGIGSVEH HSESPETYFC HTPGLKVVSC SNPNDAYWMI QQAIASSDPV IFLEPKRRYH
DKGEVDTSMA PPPLHQAKIV RSGTDVTLLS WGPMVKTCLE AAEIAAEEGR NVEVVDLRTL
SPIDTPTLLA SARRTGRVVV VHEAYKTLGL GAELAARISQ ECYFELEAPV LRVTAPDIAY
PPSRVEEDYL PTLDRVLDAV DESLSY
//
