ID F6GIZ1_LACS5 Unreviewed; 667 AA.
AC F6GIZ1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), Pyruvate dehydrogenase (Acetyl-transferring) {ECO:0000313|EMBL:AEH02380.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:AEH02380.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:AEH02380.1};
GN OrderedLocusNames=Lacal_2539 {ECO:0000313|EMBL:AEH02380.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH02380.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH02380.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH02380.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP002825; AEH02380.1; -; Genomic_DNA.
DR AlphaFoldDB; F6GIZ1; -.
DR STRING; 983544.Lacal_2539; -.
DR KEGG; lan:Lacal_2539; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_10; -.
DR OMA; PMHRNLG; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000008297; Chromosome.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AEH02380.1}; Pyruvate {ECO:0000313|EMBL:AEH02380.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008297}.
FT DOMAIN 350..523
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 74605 MW; BB64C2AA14366BCC CRC64;
MPNTLMKSNI NYNKTKLSSK TKIALYQAML KPRLIEEKML ILLRQGKISK WFSGIGQEAI
SVGVTMAMHA EEYILPMHRN LGVFTTRDIP LYRLFSQWQG KANGFTKGRD RSFHFGTQEF
NIVGMISHLG PQFGVADGIA LASKLKNKNQ VTAVFTGEGG TSEGDIHEAL NVASVWQLPV
LFCIENNGYG LSTPTKEQYN CENLADRALG YGMESHIIDG NNILEVFTKI SKITESIRKK
PRPVLIEFKT FRMRGHEEAS GTKYVPQELM DQWAKKDPID NYKLHLLEEG ILTEKEDAIF
KAEIKAEIDT HLDRTNAEAA IVSTESNELN DVFKSFDYQG VKENKNTEEL RLIDAIHVGL
KQSMEKHKDL VIMGQDVAEY GGVFKITDGF VEAFGKDRVR NTPICESAII ETAMGLSIAG
IKSVVELQFS DFVTSGFNPV VNYLAKSHYR WNQNADVVLR MPCGAGVAAG PFHSQTNEAW
FTKTPGLKVI YPAFPKDAKG LLATAINDPN PVLFFEHKAL YRSIRQDVPT DYFTIPFGKA
ATLKQGDDIT VIAYGQAVHW ALNTLDKHQD ISADVIDLRS LQPLDTETIY ASAKKTGRVI
ILQEDSLFGG IASDISALIM ENCFEHLDAP VKRVASLETP IPFINQLEDQ YLARDKFEAE
LLTLLEY
//