ODBA_DICDI
ID ODBA_DICDI Reviewed; 441 AA.
AC Q54M22;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE Short=BCKDE1A;
DE Short=BCKDH E1-alpha;
DE Flags: Precursor;
GN Name=bkdA; ORFNames=DDB_G0286335;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterotetramer of alpha and beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- MISCELLANEOUS: Bound potassium ions stabilize the protein structure.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64343.1; -; Genomic_DNA.
DR RefSeq; XP_637809.1; XM_632717.1.
DR AlphaFoldDB; Q54M22; -.
DR SMR; Q54M22; -.
DR STRING; 44689.DDB0230190; -.
DR PaxDb; Q54M22; -.
DR EnsemblProtists; EAL64343; EAL64343; DDB_G0286335.
DR GeneID; 8625523; -.
DR KEGG; ddi:DDB_G0286335; -.
DR dictyBase; DDB_G0286335; bkdA.
DR eggNOG; KOG1182; Eukaryota.
DR HOGENOM; CLU_029393_1_2_1; -.
DR InParanoid; Q54M22; -.
DR OMA; GMFRGVN; -.
DR PhylomeDB; Q54M22; -.
DR Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR PRO; PR:Q54M22; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0017086; C:3-methyl-2-oxobutanoate dehydrogenase (lipoamide) complex; IC:dictyBase.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR InterPro; IPR034616; BCKDH_E1-a.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 3: Inferred from homology;
KW Metal-binding; Mitochondrion; Oxidoreductase; Potassium;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..441
FT /note="2-oxoisovalerate dehydrogenase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000327985"
FT BINDING 145..147
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 50326 MW; E4ECC73ADFFC0538 CRC64;
MISQSYRILS RISRNNELKK TFLTNLNCKS SSPSIIRSFC KKQNLDENFE YTNKLEVQEL
KHYIPCYTIM DQEGVVSKPD QDPNFSKEEV IKMYTTMLTL NVMDSILYDV QRQGRISFYM
TSFGEEAIHI GSAAALEMSD TIFAQYRETG VFMWRGFTIN DIINQCCTNE HDLGKGRQMP
MHFGSRKINL QTISSPLTTQ LPQAVGSSYA QKLAGEKNCT IVYFGEGAAS EGDFHAAMNF
AAALSTPTIF FCRNNKWAIS TPSKEQYKGD GIAGRGPNGY GMKTIRVDGN DIWAVYNVTK
LARKIAVEEQ VPVLIEAMTY RVGHHSTSDD SSRYRTVEEI NAWKEGKNPI SRLRNYMNHK
GWWSDAQEKE TIANARTTVR ESLVNAEKQY KPSINEIFTD VYDKPTPNLI EQQKELIEHL
KLYPDEYPLN QFADSKLILK D
