ID A0A200QH48_9MAGN Unreviewed; 475 AA.
AC A0A200QH48;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=BVC80_9101g327 {ECO:0000313|EMBL:OVA09782.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA09782.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA09782.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA09782.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OVA09782.1}.
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DR EMBL; MVGT01002051; OVA09782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QH48; -.
DR STRING; 56857.A0A200QH48; -.
DR InParanoid; A0A200QH48; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR NCBIfam; TIGR01347; sucB; 1.
DR PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 99..174
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 14..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51681 MW; 4DDEDF064F96C811 CRC64;
MWSVVRRKIA SEGSNASSNL GQSLHKLRPT ASTTRSYTAA SKETLIRGRG SKHVRNFSRH
ILPGVPVSSK PMREVAGLLQ KDSPLRMWSR SFSSDNGDLV EAVVPYMGES ITDGTLAAFL
KKPGDSVQVD EPIAQVETDK VTIDVASPEA GVIQKFVAKE GDTVEPGTRI AVISKSADGV
THVAPSEEKK SVKDTPKPSA PAEKDVMAKQ KSTVESAAVK EKPKAPSPAP SRTTATEPIL
PPKERERRVP MTRLRKRVAT RLKDSQNTFA LLTTFNEVDM TNLMKLRSDY KDAFVEKHGV
KLGFMSGFVK AAVSGLQNQP IINAVIDGDD IIYRDYIDIS IAVGTPKGLV VPVIRNADQM
NFADIEKEIN SLAKKANDGT ISIDEMAGGS FTISNGGVYG SLLSTPIINP PQSAILGMHS
IVSRPMVVGG NVVPRPMMYI ALTYDHRLID GREAVFFLRR IKDVVEDPRR LLLDI
//
