ID I0AK51_IGNAJ Unreviewed; 702 AA.
AC I0AK51;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:AFH49358.1};
GN Name=bkdA {ECO:0000313|EMBL:AFH49358.1};
GN OrderedLocusNames=IALB_1650 {ECO:0000313|EMBL:AFH49358.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49358.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH49358.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP003418; AFH49358.1; -; Genomic_DNA.
DR RefSeq; WP_014560511.1; NC_017464.1.
DR AlphaFoldDB; I0AK51; -.
DR STRING; 945713.IALB_1650; -.
DR GeneID; 78243310; -.
DR KEGG; ial:IALB_1650; -.
DR PATRIC; fig|945713.3.peg.1651; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_10; -.
DR Proteomes; UP000007394; 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 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:UP000007394}.
FT DOMAIN 376..552
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 702 AA; 78219 MW; 6F19800043453303 CRC64;
MTKKTNTQKT KVKSSLKPTN GKSMIAKIKA GNKEFTKDEL LHVLRMMLRT RTLDNKAMNL
LRQGKTFFHI AASGHEAVQV AIGLSLNPNK DWLFPYYRDL GTVLTSGITP EEVFLQTFAK
ATDPASGGRQ LPVHWGSKRI NLPTQSSPTG TQFLQAVGTA LASVKRGERN ISYVSSGEGT
TSQGEFHEAV NWASREKLPV LFVIQNNKYA ISVPVSAQSG GKGHSIAEMM AGFGTLHRLK
IDGTDFFESY EKIQEAIDYI KSGKGPALIE AEVVRLQSHS SSDDQKKYRD EKEIEEDMKK
CPIEKFAKVL MTKGILTEEE YSEIKKEITD EINEASDRAF KAPDPKPEDA TKFVYDESGF
KESLEYEKNE PSGNKIVMVD AINHALHEEM ERNPDMYIFG EDIEDGKGGV FTATKGLSTR
FTRKRVFNSP LAEASIMGVA IGMAFTGLKP VVEIQFGDYI WPAFMQMKDE LATIRYRSNN
AWETPVVTRV AVGGYIHGGL YHSQNIESIF AHVPGIFIAY PSNAADAKGL LKTACRIKDP
VLFCEHKGLY RQSFAMSPEP DEEYLIPFGK AKVAKEGSDV TVVSWGVSFW DAMIAAKKLE
EENGYSVEVI DIRTIIPLDE DTIYNSVKKT NKVIIIHEDT FTAGFGAEIA ARISDYCFRF
LDAPVKRIAA KDAHIPYSPI LENAVLPSRD EIYKGIKDLI LY
//
