ID A0A1N7LAX0_9BACT Unreviewed; 804 AA.
AC A0A1N7LAX0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:SIS70880.1};
GN ORFNames=SAMN05421761_103175 {ECO:0000313|EMBL:SIS70880.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIS70880.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIS70880.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIS70880.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTOP01000003; SIS70880.1; -; Genomic_DNA.
DR RefSeq; WP_076499089.1; NZ_FTOP01000003.1.
DR AlphaFoldDB; A0A1N7LAX0; -.
DR STRING; 529505.SAMN05421761_103175; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000186026; 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 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:SIS70880.1}.
FT DOMAIN 471..645
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 804 AA; 89552 MW; 1AA363711F578CA7 CRC64;
MTEVASAAKN KKQKALKKEQ LLKDYRIAQE SRQASLMGRK EVFMGKAKFG IFGDGKELAQ
LAMARYFQNG DFRAGYYRDQ TFMFAINQLT VQEYFAQLYA HTDVEADPAS AGRLMNGHFA
TRSLNDDGTW KNLAEMKNSS ADISPTAAQM PKLLGLAYAS KLFRENEGLH GLTQFTNKGN
EVAWGTIGNA STSEGMFFES INAAGVLQVP MVVSVWDDGY GISVPNEYHT TKGSISEILK
GLQRNDDQKG YEIFVVKGWD YEALDRAFEN AARIAREEHV PVLIHVVEVT QPQGHSTSGS
HERYKSPERL QWEKEHDCIL KFREFLLDRG VASEEELGQI DAEAKQYVKD QKEAAWKAFA
GTIKSELDEA VALLKETATN SSNPSGINQL AEELSKTLNP IRKDVISTVR RALWMLRTDS
ETVKANLRDW YTAQQKLNED RYSSHLYSES EFKVENIASV PAIYAEDAPL VDGREILQAC
FDDLLTRDPR FFAFGEDVGK IGDVNQAFAG LQAKHGELRV TDTSIRECTI IGQGLGAALR
GLRPMAEIQY LDYIYYALMT LADDVASLQY RTKGGQKAPL IVRTRGHRLE GVWHAGSPIG
MLLHSLRGML LCVPRDMTQA AGMYNTLMEA DEPALVIECL NGYRLKEKMP SNISEMKVPL
GLPEILRAGT DLTIVTYGSM CRIVMDAAEE LALMGIDVEV IDVQTLLPFD TTGVIGRSIQ
KTNRVLFADE DVPGGASAYM MQQVIEGQNA YYHLDSEPAT IAAKAHRPAY SSDGDYFSKP
SIEDIVEKVY AMMHEVNPAK FPQI
//
