ODBB_PSEPU
ID ODBB_PSEPU Reviewed; 339 AA.
AC P09061;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE Short=BCKDH E1-beta;
GN Name=bkdA2;
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 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 -!- SEQUENCE CAUTION:
CC Sequence=AAA65615.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M57613; AAA65616.1; -; Genomic_DNA.
DR EMBL; M57613; AAA65615.1; ALT_INIT; Genomic_DNA.
DR PIR; S01318; DEPSEB.
DR PDB; 1QS0; X-ray; 2.40 A; B=2-339.
DR PDB; 2BP7; X-ray; 2.90 A; B/D/F/H=1-339.
DR PDBsum; 1QS0; -.
DR PDBsum; 2BP7; -.
DR AlphaFoldDB; P09061; -.
DR SMR; P09061; -.
DR DIP; DIP-6209N; -.
DR IntAct; P09061; 1.
DR STRING; 1240350.AMZE01000027_gene4713; -.
DR eggNOG; COG0022; Bacteria.
DR EvolutionaryTrace; P09061; -.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Thiamine pyrophosphate.
FT CHAIN 1..339
FT /note="2-oxoisovalerate dehydrogenase subunit beta"
FT /id="PRO_0000162251"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 8..22
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 98..102
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1QS0"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2BP7"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1QS0"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:1QS0"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:1QS0"
SQ SEQUENCE 339 AA; 37134 MW; 318FE1E403B2AEA5 CRC64;
MATTTMTMIQ ALRSAMDVML ERDDNVVVYG QDVGYFGGVF RCTEGLQTKY GKSRVFDAPI
SESGIVGTAV GMGAYGLRPV VEIQFADYFY PASDQIVSEM ARLRYRSAGE FIAPLTLRMP
CGGGIYGGQT HSQSPEAMFT QVCGLRTVMP SNPYDAKGLL IASIECDDPV IFLEPKRLYN
GPFDGHHDRP VTPWSKHPHS AVPDGYYTVP LDKAAITRPG NDVSVLTYGT TVYVAQVAAE
ESGVDAEVID LRSLWPLDLD TIVESVKKTG RCVVVHEATR TCGFGAELVS LVQEHCFHHL
EAPIERVTGW DTPYPHAQEW AYFPGPSRVG AALKKVMEV
