ID A0A0Q8DMV0_9ACTN Unreviewed; 739 AA.
AC A0A0Q8DMV0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=ASD81_13475 {ECO:0000313|EMBL:KRA32549.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA32549.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA32549.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA32549.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA32549.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA32549.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRA32549.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMGV01000006; KRA32549.1; -; Genomic_DNA.
DR RefSeq; WP_056711448.1; NZ_LMGV01000006.1.
DR AlphaFoldDB; A0A0Q8DMV0; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000051699; 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:UP000051699}.
FT DOMAIN 390..571
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 739 AA; 78221 MW; 274C8A91AEBC5C40 CRC64;
METVEEFFAR SVRSWRADRP GGSIPPDGGP SVGDPALLHA LFAAQLQSRH LDYAARWLQA
QGRGHYTIGS AGHESNAALG LVARVDDPAL LHYRSGGFYA ARAARAGTSD PVRDVLLSLT
SSARDPMSGG RHKVFGHPAL HIIPQTSTIS SHLPRAVGLA YALGLARAVG HTTPWPHDAI
VICSFGDASA NHSTATGALN AASYLTRREV PCPILFVCED NRIGVSTRSP DGWPGVMLES
LPGIEYVHVD GADPATLLNR TAAAVARVRQ ARRPVVLHLD TVRFLGHAGS DTEIAYRTQG
EIVGDYERDP LLATARFLMS AGQATPEEIL AAYDDTRSRV MDAAQTALDE PHLSDRAQVM
APLALPAVSP PIPVPAATAA IGGAQDSARL TLAQSINQTL AEQLATHSEV LVFGEDVAVK
GGVYGVTRGL RKRFGAQRVF DTLLDEQTIL GVALGSALAG FVPVPEIQYL AYLHNAEDQL
RGEAASLRFF SNGQYQNGMV VRVAGLAYQR GFGGHFHNDN SVAVLRDIPG LVVAVPSHPA
DAPGLLRTCL ELARQDGRVC VYLEPIALYH VRDLVAGDSE WTAPFADAAS EGSLRPLGEV
GVYGDGADLL LVTFGNGVPM SLRASERLRE HGVATTVVDL RWLSPLPLDA VHVLAERFPA
VLVVDETRAS GGVSEGVVTG LLEHGYRGRL SRVASADSFV PLGPAAATVL LSEEDVVAAA
LSGSLRGSPL APLTARRTT
//
