ODB2_BOVIN
ID ODB2_BOVIN Reviewed; 482 AA.
AC P11181; A7YWE9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial;
DE EC=2.3.1.168;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase complex component E2;
DE Short=BCKAD-E2;
DE Short=BCKADE2;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;
DE AltName: Full=Dihydrolipoamide branched chain transacylase;
DE AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;
DE Flags: Precursor;
GN Name=DBT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3049570; DOI=10.1016/s0021-9258(18)68177-3;
RA Griffin T.A., Lau K.S., Chuang D.T.;
RT "Characterization and conservation of the inner E2 core domain structure of
RT branched-chain alpha-keto acid dehydrogenase complex from bovine liver.
RT Construction of a cDNA encoding the entire transacylase (E2b) precursor.";
RL J. Biol. Chem. 263:14008-14014(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-228.
RX PubMed=2837277; DOI=10.1021/bi00406a025;
RA Lau K.S., Griffin T.A., Hu C.-W.C., Chuang D.T.;
RT "Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl
RT dehydrogenase binding domains of mammalian branched-chain alpha-keto acid
RT dehydrogenase complex: molecular cloning of human and bovine transacylase
RT (E2) cDNAs.";
RL Biochemistry 27:1972-1981(1988).
RN [4]
RP PROTEIN SEQUENCE OF 100-109, AND LIPOYLATION AT LYS-105.
RX PubMed=3245861; DOI=10.1016/s0021-9258(18)68766-6;
RA Hummel K.B., Litwer S., Bradford A.P., Aitken A., Danner D.J., Yeaman S.J.;
RT "Nucleotide sequence of a cDNA for branched chain acyltransferase with
RT analysis of the deduced protein structure.";
RL J. Biol. Chem. 263:6165-6168(1988).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CHARACTERIZATION OF
RP COMPLEX CATALYTIC ACTIVITY.
RX PubMed=283398; DOI=10.1073/pnas.75.10.4881;
RA Pettit F.H., Yeaman S.J., Reed L.J.;
RT "Purification and characterization of branched chain alpha-keto acid
RT dehydrogenase complex of bovine kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:4881-4885(1978).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 223-482.
RX PubMed=17124494; DOI=10.1038/sj.emboj.7601444;
RA Kato M., Wynn R.M., Chuang J.L., Brautigam C.A., Custorio M., Chuang D.T.;
RT "A synchronized substrate-gating mechanism revealed by cubic-core structure
RT of the bovine branched-chain alpha-ketoacid dehydrogenase complex.";
RL EMBO J. 25:5983-5994(2006).
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). Within this complex, the catalytic
CC function of this enzyme is to accept, and to transfer to coenzyme A,
CC acyl groups that are generated by the branched-chain alpha-keto acid
CC decarboxylase component. {ECO:0000269|PubMed:283398}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-
CC CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [protein] + CoA; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:283398}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:283398}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M21572; AAA30597.1; -; mRNA.
DR EMBL; BC134527; AAI34528.1; -; mRNA.
DR EMBL; M19475; AAA30596.1; -; mRNA.
DR PIR; A30801; XUBOLA.
DR RefSeq; NP_776330.1; NM_173905.2.
DR PDB; 2IHW; X-ray; 2.70 A; A/B/C/D/E/F/G/H=223-482.
DR PDB; 2II3; X-ray; 2.17 A; A/B/C/D/E/F/G/H=223-482.
DR PDB; 2II4; X-ray; 2.59 A; A/B/C/D/E/F/G/H=223-482.
DR PDB; 2II5; X-ray; 2.50 A; A/B/C/D/E/F/G/H=223-482.
DR PDBsum; 2IHW; -.
DR PDBsum; 2II3; -.
DR PDBsum; 2II4; -.
DR PDBsum; 2II5; -.
DR AlphaFoldDB; P11181; -.
DR SMR; P11181; -.
DR IntAct; P11181; 1.
DR STRING; 9913.ENSBTAP00000008292; -.
DR PaxDb; P11181; -.
DR PeptideAtlas; P11181; -.
DR PRIDE; P11181; -.
DR Ensembl; ENSBTAT00000008292; ENSBTAP00000008292; ENSBTAG00000006320.
DR GeneID; 280759; -.
DR KEGG; bta:280759; -.
DR CTD; 1629; -.
DR VEuPathDB; HostDB:ENSBTAG00000006320; -.
DR VGNC; VGNC:27896; DBT.
DR eggNOG; KOG0558; Eukaryota.
DR GeneTree; ENSGT00940000156750; -.
DR HOGENOM; CLU_016733_10_0_1; -.
DR InParanoid; P11181; -.
DR OMA; HPCIMAP; -.
DR OrthoDB; 854035at2759; -.
DR TreeFam; TF314182; -.
DR SABIO-RK; P11181; -.
DR EvolutionaryTrace; P11181; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000006320; Expressed in liver and 106 other tissues.
DR ExpressionAtlas; P11181; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:Ensembl.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW Lipoyl; Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT CHAIN 62..482
FT /note="Lipoamide acyltransferase component of branched-
FT chain alpha-keto acid dehydrogenase complex, mitochondrial"
FT /id="PRO_0000020488"
FT DOMAIN 64..139
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 172..209
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /evidence="ECO:0000255"
FT ACT_SITE 456
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:3245861"
FT MOD_RES 133
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 196
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 196
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11182"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 261
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 289
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 289
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11182"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 440
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 440
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT CONFLICT 173
FT /note="A -> G (in Ref. 3; AAA30596)"
FT /evidence="ECO:0000305"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 285..300
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:2II3"
FT STRAND 438..451
FT /evidence="ECO:0007829|PDB:2II3"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 457..472
FT /evidence="ECO:0007829|PDB:2II3"
FT HELIX 475..480
FT /evidence="ECO:0007829|PDB:2II3"
SQ SEQUENCE 482 AA; 53410 MW; 70F06EE62B14B5C6 CRC64;
MAAALVLRTW SRAAGQLICV RYFQTCGNVH VLKPKYVCFF GYPPFKYSHP YQWLKTTAAL
QGQIVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKK
LYYNLDDTAY VGKPLVDIET EALKDSEEDV VETPAVSHDE HTHQEIKGQK TLATPAVRRL
AMENNIKLSE VIGSGKDGRI LKEDILNYLE KQTGAILPPS PKAEIMPPPP KPKDRTIPIP
ISKPPVFIGK DRTEPVKGFH KAMVKTMSAA LKIPHFGYCD EVDLTELVKL REELKPIAFA
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT EQGLIVPNVK
NVQIRSIFEI ATELNRLQKL GSAGQLSTND LIGGTFTLSN IGSIGGTYAK PVILPPEVAI
GALGTIKALP RFNEKGEVCK AQIMNVSWSA DHRIIDGATV SRFSNLWKSY LENPAFMLLD
LK
