ID   W9GQN1_9MICO            Unreviewed;       756 AA.
AC   W9GQN1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN   ORFNames=N864_12255 {ECO:0000313|EMBL:EWT07118.1};
OS   Intrasporangium chromatireducens Q5-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT07118.1, ECO:0000313|Proteomes:UP000019494};
RN   [1] {ECO:0000313|Proteomes:UP000019494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) 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:EWT07118.1}.
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DR   EMBL; AWQS01000021; EWT07118.1; -; Genomic_DNA.
DR   RefSeq; WP_051518203.1; NZ_AWQS01000021.1.
DR   AlphaFoldDB; W9GQN1; -.
DR   PATRIC; fig|584657.3.peg.936; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000019494; 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:UP000019494}.
FT   DOMAIN          413..594
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          20..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   756 AA;  80238 MW;  A38AD2F49C36979F CRC64;
     MSGPIDEHFL QEVRSWTGHL TGHTADPGTV TDSGTAAEPG DTARTGVSDA LLLDLFEAQL
     LSRHLDFAAR YLQAQGEGFY TIGSSGHESN AAVALALRPS DPALLHYRSG GFYCARAGQV
     PGSDAAADIL RSLTCSVDDP ISGGRHKVFG HPELMVIPQT STIASHVPRA LGMAFALDRR
     GPLGVATPVP GDAVVVTSLG DASVNHSTAI GALNAAGQLA HRGVPLPLLV LCEDNGIGIS
     VRTPSGWTRR TLESLPGFDY VAADGTDPEQ CLAVAAEAVE RVRTERKPVI LHLSTVRLMG
     HAGSDVELAY RSRREIERDY AADPLVATAR ALHARRVQTT DELVERYEQV RRQVEERAKR
     LMPVRRLDSA EAVMRPLTER SPAQVRAASA ASAPAAGREA AFGGKLPEDS GPLTLAQSIN
     AALTDLMALH REVVVFGEDV AAKGGVYGVT RGLRKRFGAQ RVFDTLLDEQ TILGTALGSA
     LAGFLPVPEI QYLAYLHNAE DQLRGEAATL RFFSNGQFGN GMLVRVQGLA YQKGFGGHYH
     NDNSVAVLRD IPGLVLATPS SAAEAPRLVR AMAAFAREES RVCVLLEPIA LYHTRDLAPG
     DGAWTAPYAP PETWGHDRAE PGVGATHGEG GDVLVVTFGN GVPMSLRAVA AAEERAARHG
     RSAPRTTVYD LRWLAPLPVD DLLQRARGFD RVLVVDETRR SGGVSEGVVT ALVDGGYRGA
     ISRVTSKDSI IPLGPAASTV LLSEEDIIDA LLGGTL
//