ID A0A1Q9CPR6_SYMMI Unreviewed; 615 AA.
AC A0A1Q9CPR6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=bkdA {ECO:0000313|EMBL:OLP84875.1};
GN ORFNames=AK812_SmicGene34199 {ECO:0000313|EMBL:OLP84875.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP84875.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP84875.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP84875.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-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|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:OLP84875.1}.
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DR EMBL; LSRX01001011; OLP84875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9CPR6; -.
DR OrthoDB; 952at2759; -.
DR Proteomes; UP000186817; 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:UP000186817};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 77..376
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 615 AA; 68645 MW; 105E5EECEF569A9F CRC64;
MALKATCLAA DALRRSRSSR GLATFAGLKH KARFVHEPHI HKVDPAQALP VLRLVGEDGQ
IQVDSLPCSL EQYLDMYKCM LKVSVVDQVM NSLQRQGRIS FYMTGLGEEA AQVGPAAALH
KDDVIWAQYR ELGTFMYRGF SIQQMVSQCF SRFDEPGKGR QMPVHYCDAS IGMQAITSPL
GTQIPQAVGA GYGFRISGER RVGVAFFGEG AASEGDFAVA LNFAATLQSQ VLFICRNNGW
AISTPAEEQY AGDGIAARAL AYGMSCIRVD GNDLAAVYVA TKEARELSLE GRPVLLELMT
YRQGHHSTSD DAGRYRDSGK VKSMARTGLE PISRSRLVLK EANMWDDAQE EELKGRYRQE
VMEALKVAES KPFASVKEMF RDVWAELTPE LERQREDLIA HVERHPEHYA QKWSALIGLA
ERGCGSQRDG GAVFRFEGHI AQNHFYCLRV QQAGECPANG EVRKYRESAA SSKLPAISTE
DRRRIHAAAD SLLQDFMRPT PTAVIQRLGS PPVDAAQVRS VLRWRREQHG DCTATFRASE
SDFTEEAERW ANVDSNPIYL ARWTLNIFCW AAVLTPFMLE LVRLKQTGRL DGIFIAADWT
FKVVVMKYSF LPVLI
//
