ID W5TIT2_9NOCA Unreviewed; 828 AA.
AC W5TIT2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=NONO_c44760 {ECO:0000313|EMBL:AHH19260.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH19260.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH19260.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH19260.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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; CP006850; AHH19260.1; -; Genomic_DNA.
DR AlphaFoldDB; W5TIT2; -.
DR STRING; 1415166.NONO_c44760; -.
DR KEGG; nno:NONO_c44760; -.
DR PATRIC; fig|1415166.3.peg.4599; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_11; -.
DR Proteomes; UP000019150; 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:UP000019150}.
FT DOMAIN 493..674
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 364..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 85948 MW; 8D100B52B737DA34 CRC64;
MTPEELLDDV LRSTVAAVAP GPPRRLTDPI VPGAAITAAT CLELFDAQAS SRHLDLAARR
LGSSGAGYYS IGSSGHEGNA ALAEVLRPTD PALLHYRSGA FFVRRCQRIP DLDPIRDVLL
GVVAAAADPI SGGRHKVFGS RAAAVIPQTS TIASHLPRAV GLAFALDRRR ESPWPPDAVV
LCTFGDASAN HSTATGAINT AMHTAHLGIP MPVLFVCEDN GIGISVPTPP DWIETAYGSR
PGLRYFEADG SDLLAALAVS AEAARWVRTR RRPAFLRLRT VRLLGHAGSD VESAYRGVAD
IEADRHRDPV AATARLLVTA GAATARQILD RYDALGARIA AVAAQVVDEP HLTSAAAVRA
PLAYRTTDDT ARQRREPPDH DDHPVTTADH EPASASASTP APASTPASAP APAPISASAS
APASAPASAP APAPAPAPAS ASASASASAS ASASASDAAA GLEGAAATVS GTAAKESADT
SSGSGPGEPE SRMTLAQSVN HTLAALLRHD PDILVFGEDA GRKGGVYGVT KGLQRAFGAR
RVFDTLLDEQ SVLGAALGAS LAGFVPIPEI QYLAYLHNAL DQIRGEAATL SYFSDGQYRN
PMVVRVASFA YQKGFGGHFH NDNSVAALRD IPGLVVAAPA RADDAAALLR RCAELARTEG
RVCLFLEPIA LYHTRDLYES GDSAWLAAPE EEPADFARAR IHGSGTDLTI VTFANGVRMS
LRAAQCLADN GIHARVLDLR WLTPLPAADI LHHATATGAV LVADETRRSG GVSESVCAAL
IDGGFRGRVA RVTSDDSFVP LGPAADLVLL NESAIVDAAL RLLDTRST
//
