ID A0A3Q0J629_DIACI Unreviewed; 1124 AA.
AC A0A3Q0J629;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial {ECO:0000256|ARBA:ARBA00039275};
DE EC=2.3.1.168 {ECO:0000256|ARBA:ARBA00038880};
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00042008};
GN Name=LOC113465296 {ECO:0000313|RefSeq:XP_026683891.1};
OS Diaphorina citri (Asian citrus psyllid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC Diaphorininae; Diaphorina.
OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026683891.1};
RN [1] {ECO:0000313|RefSeq:XP_026683891.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR RefSeq; XP_026683891.1; XM_026828090.1.
DR AlphaFoldDB; A0A3Q0J629; -.
DR STRING; 121845.A0A3Q0J629; -.
DR PaxDb; 121845-A0A3Q0J629; -.
DR KEGG; dci:113465296; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000079169; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 2.
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 PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 2.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000079169};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 156..233
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 316..353
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 678..755
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 838..875
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 241..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 124837 MW; CA1A3CDA30082FF4 CRC64;
MNQTNAALLN NYKCIYSTGI LKSKASRCRN ISTMCRLQLL VNTRSKFQQV LGRNKSELFH
SGSKSLPPIV SYLPKSSLIV STFRPSREFS SLIALNRTNK FESLNTKNKF DPLSSISSSL
SRKFSSSLQL RHGLHLSTPP LQCHHHLHTS CIRHKLIQFK LADIGEGIRE VNIKEWNGNV
TEGARINEFD VVCEVESDKA SVTITSRYKG TVRKVYYGEG DVALVGKPLL DIEVEDEGVA
AEEADSLDRK AAPGVSEVNT PDTSDQPNET LHKEPNKVNR EPIAHKPDVT PDLSRDSAVS
HLNQPVNLNK NKWKILATPS VRRMIKHYEI DTKELRGTGK QGRVLKEDII TYMNSPIDET
NLAHTAHVRE ASNVISIRGY VKGMFKSMTE ACDLTFKVKV HVHSITLREK MGCLQPKLGY
LHSSFGTECQ KPMFILSKPE LAEDDPMDAS GGDAPSPQPQ EPELAEDDPM DASGGDAPSP
QPQGNPSTLT PPHQTNSKPN KPKPEGRIVP SNKLQLHTTT VNMNQTNAAL SNNYKCIYST
GILKSKVSRC RNVSTMSRLQ LLVNTRSKFQ LLIGRNKPEL FHSRSKSLPP IVSYLPKSSL
IVSTFRPSRE FSSLISLNGT NKFESLNTKN RFDPLSSISS SLSRKFSSSL QLRHGHHLST
PPLQCHHHLH TSCIRHKLIQ FNLADIGEGI REVNIKEWNG NVTEGARINE FDVVCEVESD
KASVTITSRY KGTVRKVYYG EGDVALVGKP LLDIEVEDEG VAAEEADSLD RKAAPGVSEV
NTPDTSDQPN ETLHKEPNKV NREPIAHKPD VTPDLSRDSA VSHLNQPVNL NKNKWKILAT
PSVRRMIKHY EIDTKELRGT GKQGRVLKED IITYMNSPSD ETNPAHTAHV REASNVIPIR
GYVKGMFKSM TEANTIPSLR LTEEVDTTQL RDVKNQVSAL YQEKFRLKLT YMPFFIKALS
LCMTEHPILN ASIDPTQENI LVNPDHNISI AIDTKHGLVV PNIKSVNKLC LLDITRELLR
IQGCSHEGKV LPRDIQGGTI SMSNVGNVGG TLVQPIIVPG QVCIVAFGKI QLLPRFDAEM
RIVAKCILNV TWAADHRVVD GATVARAATL WKSLVENPAL LLTQ
//
