ODBA_PSEPU
ID ODBA_PSEPU Reviewed; 410 AA.
AC P09060;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE Short=BCKDH E1-alpha;
GN Name=bkdA1;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G2;
RX PubMed=3416875; DOI=10.1111/j.1432-1033.1988.tb14283.x;
RA Burns G., Brown T., Hatter K., Idriss J., Sokatch J.R.;
RT "Similarity of the E1 subunits of branched-chain-oxoacid dehydrogenase from
RT Pseudomonas putida to the corresponding subunits of mammalian branched-
RT chain-oxoacid and pyruvate dehydrogenases.";
RL Eur. J. Biochem. 176:311-317(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=G2;
RX PubMed=2211503; DOI=10.1128/jb.172.10.5655-5663.1990;
RA Madhusudhan K.T., Huang G., Burns G., Sokatch J.R.;
RT "Transcriptional analysis of the promoter region of the Pseudomonas putida
RT branched-chain keto acid dehydrogenase operon.";
RL J. Bacteriol. 172:5655-5663(1990).
RN [3]
RP PROTEIN SEQUENCE OF 1-13.
RX PubMed=8521848; DOI=10.1111/j.1432-1033.1995.828_3.x;
RA Hester K., Luo J., Burns G., Braswell E.H., Sokatch J.R.;
RT "Purification of active E1 alpha 2 beta 2 of Pseudomonas putida branched-
RT chain-oxoacid dehydrogenase.";
RL Eur. J. Biochem. 233:828-836(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10426958; DOI=10.1038/11563;
RA Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G.J.;
RT "Crystal structure of 2-oxoisovalerate and dehydrogenase and the
RT architecture of 2-oxo acid dehydrogenase multienzyme complexes.";
RL Nat. Struct. Biol. 6:785-792(1999).
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).
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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
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DR EMBL; M57613; AAA65614.1; -; Genomic_DNA.
DR PIR; S01317; DEPSXA.
DR RefSeq; WP_019099583.1; NZ_AP022324.1.
DR PDB; 1QS0; X-ray; 2.40 A; A=2-408.
DR PDB; 2BP7; X-ray; 2.90 A; A/C/E/G=1-410.
DR PDBsum; 1QS0; -.
DR PDBsum; 2BP7; -.
DR AlphaFoldDB; P09060; -.
DR SMR; P09060; -.
DR DIP; DIP-6208N; -.
DR IntAct; P09060; 1.
DR STRING; 1240350.AMZE01000027_gene4712; -.
DR PRIDE; P09060; -.
DR GeneID; 66677017; -.
DR eggNOG; COG1071; Bacteria.
DR EvolutionaryTrace; P09060; -.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:InterPro.
DR InterPro; IPR034616; BCKDH_E1-a.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR022593; Oxoisoval_DH_suAlpha_N_dom.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF12573; OxoDH_E1alpha_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Oxidoreductase;
KW Thiamine pyrophosphate.
FT CHAIN 1..410
FT /note="2-oxoisovalerate dehydrogenase subunit alpha"
FT /id="PRO_0000162249"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 74..99
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 351..373
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 399..406
FT /evidence="ECO:0007829|PDB:1QS0"
SQ SEQUENCE 410 AA; 45268 MW; 0C998460CCFB9CF4 CRC64;
MNEYAPLRLH VPEPTGRPGC QTDFSYLRLN DAGQARKPPV DVDAADTADL SYSLVRVLDE
QGDAQGPWAE DIDPQILRQG MRAMLKTRIF DSRMVVAQRQ KKMSFYMQSL GEEAIGSGQA
LALNRTDMCF PTYRQQSILM ARDVSLVEMI CQLLSNERDP LKGRQLPIMY SVREAGFFTI
SGNLATQFVQ AVGWAMASAI KGDTKIASAW IGDGATAESD FHTALTFAHV YRAPVILNVV
NNQWAISTFQ AIAGGESTTF AGRGVGCGIA SLRVDGNDFV AVYAASRWAA ERARRGLGPS
LIEWVTYRAG PHSTSDDPSK YRPADDWSHF PLGDPIARLK QHLIKIGHWS EEEHQATTAE
FEAAVIAAQK EAEQYGTLAN GHIPSAASMF EDVYKEMPDH LRRQRQELGV
