ID A0A318K0S5_9NOCA Unreviewed; 732 AA.
AC A0A318K0S5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=DFR70_12840 {ECO:0000313|EMBL:PXX53327.1};
OS Nocardia tenerifensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=228006 {ECO:0000313|EMBL:PXX53327.1, ECO:0000313|Proteomes:UP000247569};
RN [1] {ECO:0000313|EMBL:PXX53327.1, ECO:0000313|Proteomes:UP000247569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44704 {ECO:0000313|EMBL:PXX53327.1,
RC ECO:0000313|Proteomes:UP000247569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PXX53327.1}.
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DR EMBL; QJKF01000028; PXX53327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318K0S5; -.
DR Proteomes; UP000247569; 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 Pyruvate {ECO:0000313|EMBL:PXX53327.1}.
FT DOMAIN 399..580
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 732 AA; 77392 MW; 0BA07A1DFFB1262C CRC64;
MSERVASPGG SPGKILDDQF RAAVGALTPA PDRTDEIAPG VTGATLLELF EAQATSRHLD
LAARQLGASK RGYYSIGSSG HEGNAALGLA LRVNDPALLH YRSGAFFVQR ARRVAGLDPI
RDVLLGVVAA AADPISGGRH KVFGSKAAAV IPQTSTIASH LPRAVGLAFA IDRAARLGVS
SEWPSDAVVL CSFGDASANH STAAGAINAA IHTARQGVPL PILFLCEDNG IGISVPTPAD
WIQQAYGSRT GLEYFCADGC DPLDALTTSI AAAAWVREHR KPAFLHLRTV RLMGHAGSDV
EAAYRRPADI AADLLRDPVT ATARLLVATG TATPAEILAR YDDIARRVDA TAETVWQEPK
LTSAAAVVAP LAATNPALVR ADVLRAGPSE ADHGAAEPMT LGQAINRTLA DLLARDKDVL
VFGEDVGRKG GVYGVTKGLQ KQFGKRRVFD TLLDEQSVLG TALGTALAGF VPIPEIQYLA
YVHNAADQLR GEAATLAFFS EGRYRNPMVV RIAGYAYQKG FGGHFHNDNS IAALRDIPGV
VVTSPSRADD AAALLRTCVS AARVDGRVCV YLEPIALYHT RDLYEPGDNA WLATTSDIDH
AEIGRARVYG DGTDITIVTF ANGVPMSLRV ARRLSERGIR PRVLDLRWLS PLPLQDLLHH
ARATGRVLIA DETRHSGGVS ESICAALIDA GFDGYIARVT SEDSFVPLGP AADTVLLDET
KIETAAGKLL AQ
//
