ID A0A0N0AJA8_9ACTN Unreviewed; 852 AA.
AC A0A0N0AJA8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=ADK66_07525 {ECO:0000313|EMBL:KOX10734.1};
OS Micromonospora sp. NRRL B-16802.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX10734.1, ECO:0000313|Proteomes:UP000037709};
RN [1] {ECO:0000313|EMBL:KOX10734.1, ECO:0000313|Proteomes:UP000037709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX10734.1,
RC ECO:0000313|Proteomes:UP000037709};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KOX10734.1}.
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DR EMBL; LGEB01000048; KOX10734.1; -; Genomic_DNA.
DR RefSeq; WP_053653179.1; NZ_LGEB01000048.1.
DR AlphaFoldDB; A0A0N0AJA8; -.
DR STRING; 1415541.ADK66_07525; -.
DR PATRIC; fig|1415541.3.peg.1592; -.
DR OrthoDB; 4009369at2; -.
DR Proteomes; UP000037709; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
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 PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 512..693
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 116..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 88127 MW; 9903498B662755F8 CRC64;
MLCDVTTPQD LDDRFRETLA ALPAAQRRRD AADPVTDDAP LTGAQLLDLF DAQVTSRQLD
LAGRWLRSFG EGFYTIGSAG HEGNAAVAAA LRPTDPALLH YRSGAFYCVR AAQAAADAPP
TSTVEPGSTV EATSAAGPDS AARPTSTVAP APSTDVRSST EPPSGAAPST AGEPTAGPES
ADAAEGEPTG ATPPGGFEAY AEAARDVLRG MVASSQEPIA GGRHKVFGRA DLAIVPTTST
IASHLPRAVG MGLAVERLRR MDSAGRRTGA GAQVGGAENA PWPPDAIVVC SFGDASVNHA
SATAAFNTAG WYDHAGLRIP VLFVCEDNGL GISVRSPKGW VEATLRSKPG IRYFSADGAD
PVGTYAAAAE AAAWVRRHRR PAVLHLHTVR LMGHAGADAE SAYRSPAELA DDVARDPVAA
TARLLVEAGV ATGDELLARY DETGWQIRRL AEDVLGEPKL ASAAEVVSAL APRRPVRVAR
AVADAAARAS GPGAGARAEA FGGKPPELAG PLTLAQSINA ALADGMLDHP QMAVFGEDVA
AKGGVYGVTK GLRDRFGAAR VFDTLLDETS VLGLGLGAGL AGMLPVPEIQ YLAYLHNAED
QLRGEAATMQ FFSQGAFRNP MVVRVAGLAY QEGFGGHFHN DNSVSVLRDV PGLVIAVPAR
PDDAAPMLRT CLASAAVDGS VCVFLEPIAL YHTRDLYADG DGEWLAGYPE PGSWVTGHVP
IGRARVYQVG SADDLTIITF GNGVRMSLRA AAALAEEGVG TRVVDLRWLA PLPVADIIRE
SSATGRVLVV DETRRSGGVG EGVIAALVDA GYVGAARRVA GVDSFVPLGP AARQVLVSAE
AITEGARTLL AR
//
