ODB2_CAEEL
ID ODB2_CAEEL Reviewed; 448 AA.
AC Q23571;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 AltName: Full=Dihydrolipoamide branched-chain transacylase E2 {ECO:0000312|WormBase:ZK669.4};
DE Flags: Precursor;
GN Name=dbt-1 {ECO:0000303|PubMed:26683372, ECO:0000312|WormBase:ZK669.4};
GN ORFNames=ZK669.4 {ECO:0000312|WormBase:ZK669.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26683372; DOI=10.1074/jbc.m115.676650;
RA Jia F., Cui M., Than M.T., Han M.;
RT "Developmental defects of Caenorhabditis elegans lacking branched-chain
RT alpha-ketoacid dehydrogenase are mainly caused by monomethyl branched-chain
RT fatty acid deficiency.";
RL J. Biol. Chem. 291:2967-2973(2016).
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2) (By
CC similarity). It contains multiple copies of three enzymatic components:
CC branched-chain alpha-keto acid decarboxylase (E1), lipoamide
CC acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
CC Within this complex, the catalytic function of this enzyme is to
CC accept, and to transfer to coenzyme A, acyl groups that are generated
CC by the branched-chain alpha-keto acid decarboxylase component (By
CC similarity). Required for the catabolism of branched-chain amino acids
CC and the subsequent synthesis of monomethyl branched-chain fatty acids,
CC which are important for regulating postembryonic growth
CC (PubMed:26683372). {ECO:0000250|UniProtKB:P11181,
CC ECO:0000269|PubMed:26683372}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P11181}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:26683372}. Cell projection, dendrite
CC {ECO:0000269|PubMed:26683372}. Cell projection, cilium
CC {ECO:0000269|PubMed:26683372}. Note=Localizes to puncta within the
CC cytosol which is consistent with its expected location in mitochondria.
CC {ECO:0000269|PubMed:26683372}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:26683372}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC monomethyl branched-chain fatty acid generation and also results in
CC larval arrest in the subsequent generation.
CC {ECO:0000269|PubMed:26683372}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Z37093; CAA85465.1; -; Genomic_DNA.
DR PIR; T27955; T27955.
DR RefSeq; NP_495670.1; NM_063269.5.
DR AlphaFoldDB; Q23571; -.
DR SMR; Q23571; -.
DR BioGRID; 39612; 5.
DR DIP; DIP-26430N; -.
DR IntAct; Q23571; 2.
DR STRING; 6239.ZK669.4; -.
DR EPD; Q23571; -.
DR PaxDb; Q23571; -.
DR PeptideAtlas; Q23571; -.
DR EnsemblMetazoa; ZK669.4.1; ZK669.4.1; WBGene00014054.
DR GeneID; 174279; -.
DR KEGG; cel:CELE_ZK669.4; -.
DR UCSC; ZK669.4.1; c. elegans.
DR CTD; 174279; -.
DR WormBase; ZK669.4; CE01115; WBGene00014054; dbt-1.
DR eggNOG; KOG0558; Eukaryota.
DR GeneTree; ENSGT00940000156750; -.
DR HOGENOM; CLU_016733_10_0_1; -.
DR InParanoid; Q23571; -.
DR OMA; HPCIMAP; -.
DR OrthoDB; 854035at2759; -.
DR PhylomeDB; Q23571; -.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR PRO; PR:Q23571; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00014054; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Acyltransferase; Cell projection; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lipoyl;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..448
FT /note="Lipoamide acyltransferase component of branched-
FT chain alpha-keto acid dehydrogenase complex, mitochondrial"
FT /id="PRO_0000421275"
FT DOMAIN 30..105
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 146..183
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 108..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /evidence="ECO:0000255"
FT ACT_SITE 422
FT /evidence="ECO:0000255"
FT MOD_RES 71
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 448 AA; 49691 MW; E3C0FC5B2C5946AA CRC64;
MMAARLLGTS SRIFKLNKHL HTSKVAFMPV VQFKLSDIGE GIAEVQVKEW YVKEGDTISQ
FDKVCEVQSD KAAVTISCRY DGIVKKLYHE VDGMARVGQA LIDVEIEGNV EEPEQPKKEA
ASSSPEAPKS SAPKAPESAH SEGKVLATPA VRRIAIENKI KLAEVRGTGK DGRVLKEDVL
KFLGQVPADH TSGSTNIRTT HQAPQPSSKS YEPLKEDVAV PIRGYTRAMV KTMTEALKIP
HFGYNDEINV DSLVKYRAEL KEFAKERHIK LSYMPFFIKA ASLALLEYPS LNSTTDEKME
NVIHKASHNI CLAMDTPGGL VVPNIKNCEQ RSIFEIAQEL NRLLEAGKKQ QIKREDLIDG
TFSLSNIGNI GGTYASPVVF PPQVAIGAIG KIEKLPRFDK HDNVIPVNIM KVSWCADHRV
VDGATMARFS NRWKFYLEHP SAMLAQLK
