ID A0A1T1HDV3_OCELI Unreviewed; 400 AA.
AC A0A1T1HDV3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=BTA35_0200015 {ECO:0000313|EMBL:OOV87986.1};
OS Oceanospirillum linum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oceanospirillum.
OX NCBI_TaxID=966 {ECO:0000313|EMBL:OOV87986.1, ECO:0000313|Proteomes:UP000190064};
RN [1] {ECO:0000313|EMBL:OOV87986.1, ECO:0000313|Proteomes:UP000190064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV87986.1,
RC ECO:0000313|Proteomes:UP000190064};
RA Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA Mykles D.L., Maclea K.S.;
RT "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT ATCC 11336.";
RL Submitted (FEB-2017) 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:OOV87986.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTSD02000001; OOV87986.1; -; Genomic_DNA.
DR RefSeq; WP_077242396.1; NZ_MTSD02000001.1.
DR AlphaFoldDB; A0A1T1HDV3; -.
DR STRING; 966.BTA35_0200015; -.
DR Proteomes; UP000190064; 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:UP000190064};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 64..356
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 400 AA; 44660 MW; AB188CFA08DDF0E8 CRC64;
MANLKQSAKQ SEAPVVHNPV FIDGSDLTTP TLKILRQDGS VYEGAELPDI NKELALKIYD
TFQFIRALDE RMVAAQRQGR ISFYMTEIGE EAADIGSTAA LADDDMIMAQ YREQGALAFR
GFPLDQFMNQ MFSNEKDLGK GRQMPIHYGS KDLHYMTISS PLGTQLPQAV GYAYGYKLEE
KDNCVICYFG EGAASEGDFH AAINMAGVFK VPAIFFCRNN GYAISTPSSE QFAGDGIAPR
AVAYGLKAIR VDGNDVLAVL KATQEARKLA IEHNQPVLIE AMTYRLGAHS TSDDPSGYRS
KKEEEKWREK DPVLRFKHWL IQQGWWSEEQ DADIADAKRK AVMAAMKEAE KVAAPHLDDL
ITDVYDTPPK HLQEQLAELK AHIRQYPDAY PKTAGRIDHE
//
