ID L8JTV3_9BACT Unreviewed; 659 AA.
AC L8JTV3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Branched-chain alpha-keto acid dehydrogenase, E1 component, alpha subunit {ECO:0000313|EMBL:ELR72215.1};
GN ORFNames=C900_01769 {ECO:0000313|EMBL:ELR72215.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR72215.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR72215.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR72215.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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:ELR72215.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMZN01000026; ELR72215.1; -; Genomic_DNA.
DR RefSeq; WP_009579208.1; NZ_AMZN01000026.1.
DR AlphaFoldDB; L8JTV3; -.
DR STRING; 1237149.C900_01769; -.
DR PATRIC; fig|1237149.3.peg.1722; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000011135; 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:UP000011135}.
FT DOMAIN 342..515
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 659 AA; 73924 MW; FC1E6039833550E2 CRC64;
MHFDRKNYSD KILIDLYEAL LRPRMIEEKM LILLRQGKIS KWFSGIGQEA ISIGCTYPLQ
DDEYILPMHR NLGVFTTRKI PYSRLFAQFQ GKLSGFSNGR DRSFHFGTND YHIVGMISHL
GPQLAVADGI ALANMLKKEK KATLVFTGDG GASEGDFHEA LNVAAVWDLP VIFVVENNGY
GLSTPSNEQF KFKSFVDKGP GYGIDAVKID GNNVLEVYDT IRQLAENVRK NPRPVLVEAM
TFRMRGHEEA SGTKYVPTEL MEKWAKKDPL QNYEAYLLKE KVLDEATIKK IRKAIQNDIE
RGLEKAYAEE MPKASTATEI ADMYAPFEQK VVQPQSEGKN KKRYVDAISD GLKQSLEKYP
ELVIMGQDIA EYGGVFKITE GFVETFGKER IRNTPLCESA IIGIGLGMSI KKQKSVVEMQ
FADFVTCGFN QIVNNLAKSH YRWGQNADVV VRMPTGAGVA AGPFHSQSNE AWFFHTPGLK
IVYPSNPADA KGLLCAAIED PNPVIYFEHK FLYRSLTDDI HDDYYTTEIG KAKLVAAGEN
LSIITYGMGV HWAREVMESM PELSADILDL RSLLPWDKEA VAETVKKTSR VLVLHEDCMT
GGIGGEISAW ISEHCFEHLD APVMREASLD TAVPFSPPLE QNFLPKGRLQ QKIKDLVEF
//
