ID A0A1R1LRS0_9GAMM Unreviewed; 394 AA.
AC A0A1R1LRS0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=BGP75_17975 {ECO:0000313|EMBL:OMH30281.1};
OS Motiliproteus sp. MSK22-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Motiliproteus.
OX NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH30281.1, ECO:0000313|Proteomes:UP000187359};
RN [1] {ECO:0000313|EMBL:OMH30281.1, ECO:0000313|Proteomes:UP000187359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH30281.1,
RC ECO:0000313|Proteomes:UP000187359};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL Submitted (AUG-2016) 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}.
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:OMH30281.1}.
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DR EMBL; MIEQ01000061; OMH30281.1; -; Genomic_DNA.
DR RefSeq; WP_076720244.1; NZ_MIEQ01000061.1.
DR AlphaFoldDB; A0A1R1LRS0; -.
DR STRING; 1897630.BGP75_17975; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000187359; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000187359};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 53..349
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 394 AA; 44223 MW; 63D6B4F282CC16AE CRC64;
MKTGTKDRVV HKLNFIRGDE LQIPTYKVLK QDGSPYKGAT LPDLEQSTAL RIYKAMVRTR
VLDERMLAAQ RQGRLSFYMQ STGEEATTVG FAAALDDEDM IMAQYREQGA LVYRGFTLDE
FMNQLFSNER DYGKGRQMPI HYGSSKLHYM TISSPLATQI PQATGYAYGQ KLAGEGKCTV
TVFGEGAASE GDFHAALNMA SVLKVPVIFL CRNNGYAIST PSNEQFAADG IAPRALGYGM
HTIRVDGNDT LAVYAATVEA RRIAVEQNEP VLIESMSYRL AAHSSSDDPS GYRSKKEEEA
WASKDPLLRM KQWLFLQKWW TEEEDSKLFD AERREVLATL KEAEKRPICK LDELITDVYD
TPPTLLVEQL DQLKAHIRLY PDAYPKTSGD LDHG
//