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Database: UniProt
Entry: D5WXX3_KYRT2
LinkDB: D5WXX3_KYRT2
Original site: D5WXX3_KYRT2 
ID   D5WXX3_KYRT2            Unreviewed;       334 AA.
AC   D5WXX3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha {ECO:0000256|RuleBase:RU365014};
DE            EC=1.2.4.4 {ECO:0000256|RuleBase:RU365014};
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain {ECO:0000256|RuleBase:RU365014};
GN   OrderedLocusNames=Btus_1309 {ECO:0000313|EMBL:ADG06032.1};
OS   Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX   NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG06032.1, ECO:0000313|Proteomes:UP000002368};
RN   [1] {ECO:0000313|Proteomes:UP000002368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Bacillus tusciae DSM 2912.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG06032.1, ECO:0000313|Proteomes:UP000002368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX   PubMed=22180816; DOI=10.4056/sigs.2144922;
RA   Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA   Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA   Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA   Hugenholtz P., Eisen J.A.;
RT   "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT   tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT   gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT   Alicyclobacillaceae da Costa and Rainey, 2010.";
RL   Stand. Genomic Sci. 5:121-134(2011).
CC   -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC       the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: branched-chain
CC       alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000256|RuleBase:RU365014}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC         N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
CC         Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC         Evidence={ECO:0000256|RuleBase:RU365014};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU365014};
CC   -!- SIMILARITY: Belongs to the BCKDHA family.
CC       {ECO:0000256|RuleBase:RU365014}.
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DR   EMBL; CP002017; ADG06032.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5WXX3; -.
DR   STRING; 562970.Btus_1309; -.
DR   KEGG; bts:Btus_1309; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_1_0_9; -.
DR   OMA; LQYWGGD; -.
DR   Proteomes; UP000002368; Chromosome.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU365014};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT   DOMAIN          23..323
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          104..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  36255 MW;  082F754F9AA69151 CRC64;
     MSVEMRNRHE ALGLTGEDLL AMYRVMLTAR RVDERLWVLN RAGKIPFVIS CQGHEGAQVG
     AAFALDRQKD YVLPYYRDVA VVLAFGQTPR DLLLAAYAKA DDPNSGGRQM PNHFGSRKHR
     IVSGSSPVST QIPHAAGIAL AAKMRGDDVV AYVSFGEGSS NQGDFHEGLN FAAVHRLPVV
     FFCQNNGYAI SVPASKELAT PSVADRAAGY GIPGVVVDGS DVLGVYHAVK TAVERARRGD
     GPTLVEAMTV RLTPHSSDDD DRTYRSGEEL EDARRRDPLP QLAEYLIASG VADEVLLRAL
     DQEVRAEVDE ATAYAEQARD PDPADVLRFV HGEA
//
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