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Database: UniProt
Entry: A0A0F4Q823_PSEO7
LinkDB: A0A0F4Q823_PSEO7
Original site: A0A0F4Q823_PSEO7 
ID   A0A0F4Q823_PSEO7        Unreviewed;       405 AA.
AC   A0A0F4Q823;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   Name=bkdA1 {ECO:0000313|EMBL:ATD06502.1};
GN   ORFNames=PPIS_a1368 {ECO:0000313|EMBL:ATD06502.1};
OS   Pseudoalteromonas piscicida.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43662 {ECO:0000313|EMBL:ATD06502.1, ECO:0000313|Proteomes:UP000016521};
RN   [1] {ECO:0000313|EMBL:ATD06502.1, ECO:0000313|Proteomes:UP000016521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 20779 {ECO:0000313|EMBL:ATD06502.1,
RC   ECO:0000313|Proteomes:UP000016521};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011924; ATD06502.1; -; Genomic_DNA.
DR   RefSeq; WP_010372716.1; NZ_PNEL01000030.1.
DR   AlphaFoldDB; A0A0F4Q823; -.
DR   STRING; 43662.TW75_10985; -.
DR   InParanoid; A0A0F4Q823; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000016521; Chromosome i.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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          56..363
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   405 AA;  44681 MW;  3E6576C5DD402089 CRC64;
     MTNPNNISLN ISHALEFIDG HALNIPTLKI LSDQGDVLDG ATAPDIDKET ALRIYSTMRF
     IRLLDERMQG AQRQGRISFY MQCLGEEAAV TASAAALKED DMIMAQYREQ AAIHYRGFSL
     EQFMNQLFSN EKDLGKGRQM PVHYGSKELH YLTISSPLGT QIPQATGYAY GQKLKHIDKE
     TGELTSEIDN VTICYFGEGA ASEGDFHAGL NMAAVHGSPV IFYARNNGYA ISTPADEQFK
     GDGIAARGVG YGIKTIRVDG ADALAVYAAT QAARKIAVEN GEPVMIESIA YRLGAHSTSD
     DPSGYRTKDE EAEFKNSCPV NRFKQWLLKQ GWLDEAQDDA EKEKIREDIL AALKVAEKVQ
     KPALEDLVSD VYDTPIPSLQ KQYDELKAHI KAYPDAYPVT AGRIK
//
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