ID A0A0D3LCF8_9BACT Unreviewed; 803 AA.
AC A0A0D3LCF8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit {ECO:0000313|EMBL:AHM59387.1};
GN ORFNames=D770_05620 {ECO:0000313|EMBL:AHM59387.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM59387.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM59387.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM59387.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-2012) 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; CP004371; AHM59387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3LCF8; -.
DR STRING; 1257021.D770_05620; -.
DR KEGG; fbt:D770_05620; -.
DR PATRIC; fig|1257021.3.peg.1296; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000064112; Chromosome.
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 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 Pyruvate {ECO:0000313|EMBL:AHM59387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064112}.
FT DOMAIN 469..643
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 803 AA; 90254 MW; D5D0D972118F3CA8 CRC64;
METMGTYTAI ETETISLTAE EVIADYRLAQ ASRQASLMGR KEVFMGKAKF GIFGDGKETA
QIAMAKAFKA GDFRSGYYRD QTFMFAIGEL TIQQYFAQLY AHPDEEADPA TAGRLMNGHF
ATRLINEKGE WKELSKLKNS SADISPTAAQ MPRLLGLAYA SKMYRQNPDL HEFEQFSING
SEVAFGTIGD ASTSEGLFWE TINAAGVLQV PMLVGVWDDG YGISVPKEYH TTKGSISEVL
SGFQRTDTES GYEIFRVKGW DYIGLIDTFQ KAARICREEH VPVLVHVTEL TQPQGHSTSG
SHERYKPKER LQWEAEHDCL VKMREWILEN ELATEEELNE IDRDALAIAK TEKNKAWQEF
QAPIAQNQQE AEALLQEVAP LNPAITGLLE ELRKVVNPVR FDTIRAVKRA LWHLRDDNSS
AKQKIQHWME RIMQENKERF NSHLYSQSAE SALLVEGVEA EINEEDPLVD GREVLRACFD
AMFDRDPRVL AFGEDVGFIG DVNQTFAGLQ AKYGELRITD TGIREATIIG QGIGLALRGL
RPIAEIQYLD YILYGLQTLS DDLASLHYRT KGGQKAPVIV RTRGHRLEGV WHSGSPIGML
LHSLRGMHVL VPRDMTQAAG FYNTLLEADE PAVVIECLNG YRLKERVPRN IADFKVPLGV
PEILREGSDV TVVTYGSMCR VVMDAAEHLQ EFGISCEVID VQSLLPFDVH HRILESLKKT
NRIVFTDEDV PGGATAYMMQ EVIEKQGGYF HLDSQPLTLS AKAHRPAYST DGDYFSKPNI
ESVVESVYRL MNEADPQRFP KLY
//
