ID A0A2S4NAI9_9FLAO Unreviewed; 801 AA.
AC A0A2S4NAI9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase E1 component {ECO:0000313|EMBL:POS02719.1};
GN ORFNames=Q361_10229 {ECO:0000313|EMBL:POS02719.1};
OS Flavobacterium croceum DSM 17960.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121886 {ECO:0000313|EMBL:POS02719.1, ECO:0000313|Proteomes:UP000237056};
RN [1] {ECO:0000313|EMBL:POS02719.1, ECO:0000313|Proteomes:UP000237056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17960 {ECO:0000313|EMBL:POS02719.1,
RC ECO:0000313|Proteomes:UP000237056};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial
RT genomes (KMG-I) project.";
RL Submitted (JAN-2018) 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:POS02719.1}.
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DR EMBL; PQNY01000002; POS02719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4NAI9; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000237056; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:POS02719.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237056}.
FT DOMAIN 467..641
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT COILED 325..381
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 801 AA; 89998 MW; FA20494C65AB6C86 CRC64;
MTEVENKDSI TFDDFKAEVL NDYKLARISR ECSLLGRKEV LTGKAKFGIF GDGKEVPQLA
MAKAFKNGDF RSGYYRDQTF MMAIGALTPQ QFFAGLYGHI DLELEPMSAG RQMGGHFATH
SLDEHGNWKN LTKQKNSSSD ISPTAGQMPR LLGLAQASKI YRNIKNITNA DLFSINGNEI
AWGTIGNAST SEGLFFETIN AAGVLQVPMV MSVWDDEYGI SVHAKYQTTK ESISEILKGF
QRDSENNGYE IFTVKGWDYP ALVDTYQKAS QIAREEHVPV LIHVDELTQP QGHSTSGSHE
RYKNEERLAW ETQFDCVAQM RSWMIENNLA TSEELEEIEN EAKKEVNEAK KQAWLNFITP
IKNEQKELET ILLQVASTSE NKVFIEKMAR DIGSIKEPIR KELLVTARKV LRMVIHENGR
SIITHWISNY FNAIQPKYSS HLESESQNKA TSIQEIAPSY SNECEEVDAR LIIRDNFDAI
FTQYPEALIF GEDSGNIGDV NQGLEGLQEK YGELRVSDVG IREASILGQG IGMAMRGLRP
IAEIQYLDYL LYALQIMSDD LATLQYRTHG RQKAPVIIRT RGHRLEGVWH SGSPMGMILN
AVRGIHVLVP RNMTKAAGFY NTLLMSDEPA LVVECLNGYR LKEKMPNNIG AFTTAIGVVE
TIKQGVDITL VSYGSTLRLV EQAANELESI GISAEIIDVQ SLLPFDIHHD IVKSVSKTNR
LLIIDEDVPG GASAYILQKI LEEQNAYQYL DSKPHTLTAK AHRPAYGTDG DYFSKPSSED
IFEKVYEIMH EAMPYKFSKL Y
//
