ID A0A248YW57_9ACTN Unreviewed; 859 AA.
AC A0A248YW57;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=CIK06_21260 {ECO:0000313|EMBL:ASW57888.1};
OS Plantactinospora sp. KBS50.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Plantactinospora.
OX NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW57888.1, ECO:0000313|Proteomes:UP000216795};
RN [1] {ECO:0000313|EMBL:ASW57888.1, ECO:0000313|Proteomes:UP000216795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS50 {ECO:0000313|EMBL:ASW57888.1,
RC ECO:0000313|Proteomes:UP000216795};
RA Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT "Genome sequencing and analysis of secondary metabolite biosynthetic
RT capabilities of Plantactinospora sp. KBS50.";
RL Submitted (AUG-2017) 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};
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DR EMBL; CP022961; ASW57888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248YW57; -.
DR KEGG; plk:CIK06_21260; -.
DR OrthoDB; 4009369at2; -.
DR Proteomes; UP000216795; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000216795}.
FT DOMAIN 519..700
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 145..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 90032 MW; 965F293154BAFE27 CRC64;
MGNAVPRDHP QDLDERFREA VAALPGPTRE RSPAEPVRPD AALTGARALE LFDAQVTSRH
LDLAARWLRS FGEGFYTISS AGHEGNAAVA AALRPTDPAL LHYRSGAFYC VRVGQADPAE
PAEPGGRTPQ TPQTPELVIE FGRAGADEPD GTRTDDAEAA DVPPDTVDAP WDPVRADPAG
TDPAGTDPAG THPAGTDPAG GHPAAAPPRA PAPDPVQLPG WIGNAARDVL RGVVASAREP
IAGGRHKVFG NAELAVVPTT STIASHLPRA VGIGLAIERQ RRLASGSPWP ADAVVVCSFG
DASVNHASAT AALNTAGWCD HTGLRVPVLF VCEDNGLGIS VRSPRGWVEA TLRARPGLRY
FAADGGDLGQ AYDVAADAVA WVRRHRRPAV LHLTTVRLLG HAGADAEQAY GRAAELARDL
DRDPLLATAA LLVDAGLASP DDLLARYDEI GWQVRRVAEE VLGEEKLTGA AEIVAPLAPR
RPAHTVRAVA ETAERAAGSG ADARAAAFGD RLPEREGPLT LARAINATLT DAMLDNPAIA
LFGQDVAIKG GVYGVTKGLR GRFGAPRVFD TLLDETSVLG LALGAGLTGL LPVPEIQYLA
YLHNAEDQLR GEAATMRFFS RDAYRNPMVV RIAGLAYQEG FGGHFHNDNS VAVLRDVPGL
VVAVPARPDD AAAMLRTCLA SAQVDGSVCV FVEPIALYHT RDLYADGDGG WLADYPPPQQ
WPDRHAPIGR ARVYGVGTAA DLTIITFGNG VRMSLRVAAR LAAEGVGSRV VDLRWLAPLP
VADLVREATA TGRVLVVDET RRSGGVAEGV IAALVDAGYV GSVRRVASVD SFIPLGPAAR
QVLVTEDAIT EGAQMLLAG
//
