ID M0IN98_9EURY Unreviewed; 348 AA.
AC M0IN98;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000313|EMBL:ELZ96939.1};
GN ORFNames=C440_04158 {ECO:0000313|EMBL:ELZ96939.1};
OS Haloferax mucosum ATCC BAA-1512.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=662479 {ECO:0000313|EMBL:ELZ96939.1, ECO:0000313|Proteomes:UP000011550};
RN [1] {ECO:0000313|EMBL:ELZ96939.1, ECO:0000313|Proteomes:UP000011550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1512 {ECO:0000313|EMBL:ELZ96939.1,
RC ECO:0000313|Proteomes:UP000011550};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ96939.1}.
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DR EMBL; AOLN01000006; ELZ96939.1; -; Genomic_DNA.
DR RefSeq; WP_008318528.1; NZ_AOLN01000006.1.
DR AlphaFoldDB; M0IN98; -.
DR STRING; 662479.C440_04158; -.
DR PATRIC; fig|662479.7.peg.856; -.
DR OrthoDB; 25266at2157; -.
DR Proteomes; UP000011550; 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 GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:ELZ96939.1}.
FT DOMAIN 27..311
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 237..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 38985 MW; 61E7FBD6D10B2DB3 CRC64;
MHRLIAERGL DGTGFTAEDA RAALRDMIRA RRFDERALAL QRRGWMSGYP PFRGQEASQI
GAAHAMREND VLLPTYRSNA FQIARGVPPS DLLLFRRGYA EYNSDHDVPV FPQAVPIASQ
IPHAAGVGMA ADYRDDDYAA LVCFGDGATS EGDFHEGLNF AGVFDAPVVF FCENNGWAIS
LPRNRQTASE SIAAKAEAYG IEGMQVDGND PLAVRGAVEE GLEKARNGEP VLIESLTYRQ
GPHTTADDPS RYRDDDPDLP EWRTRDPVER FEEFCRDHDI ADDDRIESMY DDANDELAEA
VERAEETPEP GTEELFDYIY EDLPPELARQ REEHVEFAAE HGPFDLER
//
