ID A0A1G7DNW4_9NOCA Unreviewed; 737 AA.
AC A0A1G7DNW4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=SAMN05444580_12027 {ECO:0000313|EMBL:SDE53233.1};
OS Rhodococcus tukisamuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=168276 {ECO:0000313|EMBL:SDE53233.1, ECO:0000313|Proteomes:UP000199417};
RN [1] {ECO:0000313|EMBL:SDE53233.1, ECO:0000313|Proteomes:UP000199417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11308 {ECO:0000313|EMBL:SDE53233.1,
RC ECO:0000313|Proteomes:UP000199417};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNAB01000020; SDE53233.1; -; Genomic_DNA.
DR RefSeq; WP_072846781.1; NZ_FNAB01000020.1.
DR AlphaFoldDB; A0A1G7DNW4; -.
DR STRING; 168276.SAMN05444580_12027; -.
DR Proteomes; UP000199417; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199417}.
FT DOMAIN 403..584
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 737 AA; 77359 MW; 6DEC6EAE3449C1E6 CRC64;
MAESIDEQFV ETVGAMVSPT PGRSPAPTAP VREGSALTAA RCLELFDAQL GSRHLDLAAR
ELRARGQGYY TIGSAGHESN AAVAGALRPT DPALLHYRSG AFFLERARQV GGEAGLHDAL
RDVLLGVVAA AADPISGGRH KVFGREDLAV IPQTSTVASH LPRAVGVAFA LGRVPRLGVV
PRWPVDSVVV CSFGDASANH STAVGAINTA ANTAFRGLPM PLLLVCEDNG LGISVPTPPG
WVEAAYSGRA GLEYLAVDGA DLAGTFDAAR YAAGRVRGRR RPVFLHLRTV RLMGHAGSDV
ESAYRTPAEI GADERRDPLS AAARLLVESG LLTPAEVLDR YRLMRSRVRA LADEVAGEPR
LLTAAAVTAP LAPPDPGAVA AAVDSVRRSS SGAEELVEPA ASLTVAQAIN RALGDILAHC
REALVFGEDV GRKGGVYGVT RGLAARFGAA RVFDTVLDEQ AILGLAAGAG LSGLLPIAEI
QYLAYLHNAE DQIRGEAATL AFFSDGRYRN PMVVRVAAYG YQKGFGGHFH NDDAVAVLRD
IPGIVVASPA RPDDAAAMLH TCTAAARASG AVCVVLEPIA RYHTRDLYEP GDGQWSAPYP
PASSHVPIGR GRTYGSGRDL TIATFGNGLF LSLRAARRLQ RRGVEARVLD LRWLIPLPVE
DLLREASATG RVLVADETRR SGGVSEGVLA ALVDHGFAGA MDRVASADSF VPLGDAARLV
LLSEDEIVDA AEALVRR
//
