ID A0A1M6UED1_9FLAO Unreviewed; 803 AA.
AC A0A1M6UED1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:SHK67536.1};
GN ORFNames=SAMN04488007_3609 {ECO:0000313|EMBL:SHK67536.1};
OS Maribacter aquivivus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=228958 {ECO:0000313|EMBL:SHK67536.1, ECO:0000313|Proteomes:UP000184314};
RN [1] {ECO:0000313|EMBL:SHK67536.1, ECO:0000313|Proteomes:UP000184314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16478 {ECO:0000313|EMBL:SHK67536.1,
RC ECO:0000313|Proteomes:UP000184314};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQZX01000003; SHK67536.1; -; Genomic_DNA.
DR RefSeq; WP_073246785.1; NZ_FQZX01000003.1.
DR AlphaFoldDB; A0A1M6UED1; -.
DR STRING; 228958.SAMN04488007_3609; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000184314; 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:SHK67536.1}.
FT DOMAIN 469..643
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 803 AA; 90496 MW; 69B97B59F28F0D01 CRC64;
MDVSSKTSND ISFEDFKEQI INDYEIAFLS RTCSLLGRKE VLTGKAKFGI FGDGKELPQL
AMARSFKNGD FRSGYYRDQT FMMALGLLQP KEFFHALYAT TDIEKEPMSA GRQMGGHFLT
HSLNADGSWK DLTKQKNSSG DISCTAGQMP RLLGLAQASK VYRNQKGLDS AKFSVNGNEI
AWGTIGNAST SEGMFFETIN AAGVLQVPMV ISVWDDEYGI SVPAKFHTTK ENISEILSGF
QRTETEKGYE ILRVKGWDYT ALMHAYENAA DIARQEHVPV LIHVNELTQP QGHSTSGSHE
RYKDNQRLEW ERDHDCNKRF KEWILESGIA TSEELESIEK RIKRTVREAK KQAWDEYLKD
NLTEKSVLIN IIEKAASKSA NKNFLNKLKN DLISVEEPLR KDLAISARKS LRYLLGENTQ
EKEDLIQWTS TFLKESQHKF SSYLYSENDN KATNVTAISP AYNDDEELVD GRVILRDNFD
KLFEKYPNTL IFGEDTGAIG DVNQGLEGMQ EKYGKIRVAD TGIRETTIIG QGIGMALRGL
RPIAEIQYLD YIFYALSTLT DDLATLLYRT AGKQKAPLII RTRGHRLEGI WHSGSEMGGL
IHLLRGMYIL APRNMTQAAG FYNTLLKSDE PALVIESLNG YRLKEKKPKN LGEFCTPIGR
VETIKEGSDI TLVSYGSTLR IVEKAAKELI EVGIDAEVID AQTLLPFDIE MEVLESVKKT
NRLLVIDEDV PGGCSAYLLN EIVEKQGAFE YLDSKPQTLS AKAHRPAYGT DGDYFSKPNR
EDIFEKVYAI MHEVNPDDYP KLR
//
