ID A0A1Q6A488_9SPHI Unreviewed; 629 AA.
AC A0A1Q6A488;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=2-oxoisovalerate dehydrogenase subunit beta {ECO:0000313|EMBL:OKS88831.1};
GN ORFNames=RG47T_4309 {ECO:0000313|EMBL:OKS88831.1};
OS Mucilaginibacter polytrichastri.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS88831.1, ECO:0000313|Proteomes:UP000186720};
RN [1] {ECO:0000313|EMBL:OKS88831.1, ECO:0000313|Proteomes:UP000186720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG4-7 {ECO:0000313|EMBL:OKS88831.1,
RC ECO:0000313|Proteomes:UP000186720};
RA Li Y.;
RT "Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
RT isolated from the moss sample.";
RL Submitted (NOV-2016) 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:OKS88831.1}.
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DR EMBL; MPPL01000001; OKS88831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6A488; -.
DR STRING; 1302689.RG47T_4309; -.
DR Proteomes; UP000186720; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000186720}.
FT DOMAIN 312..485
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 629 AA; 69684 MW; CFBFB692425ED091 CRC64;
MLVLLRQGRI GKWFSGIGQE AISVGSTLAM QPDEFILPMH RNLGVFTARN IPLFNLMAQW
QGKAAGFTKG RDRSFHFGTH HYKIVGMISH LGPQMAVATG IALADVLAGR KKATLVFTGD
GATSEGDFHE AINVAAVWNL PVIFLIENNG YALSTTTGEQ YKCENLVDRA KGYGIEGRQI
DGNNLLEVYH TINELATDIR KNPRPVLIEC MTFRRRGHEE ASGVKYVPEH LFETWKAKDP
VTCYEQFLID EKILQPAWVS HTHNEFIPII EAEVEKALQQ PAIIPDVQTE LNDMYRAHTL
APAIINSSST PKRYMDAISD ALRLSMRNFP KLVLMGQDIA GYGGVFKITD GFMNEFGKER
VRNTPLCESA ILGAGLGLAI NGYKSVIEMQ FADFVSVGFN QIINNLAKSH YRWGQNADVV
IRMPAGAGTG AGPFHSQSNE AWFTKTPGLK VVYPSTPADA KGLLMAAIDD PNPVIYFEHK
YLYRTLTDEV PEGDYYVEIG KAKTVSEGND VTIITYGLGV RWALDYAKKY PDLSIEIIDL
RSLQPWDKEA AIAGVKKTGR VLVLHEDTLG SGFGAEIAAT LSECCFNYLD APIMRCASLD
TAIPMDAGLE KQFLANARLE EMMEKLLRY
//