ID A0A2T7T7F1_9ACTN Unreviewed; 1150 AA.
AC A0A2T7T7F1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN Name=kgd {ECO:0000313|EMBL:PVE11084.1};
GN ORFNames=Y717_18315 {ECO:0000313|EMBL:PVE11084.1};
OS Streptomyces scopuliridis RB72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE11084.1, ECO:0000313|Proteomes:UP000245992};
RN [1] {ECO:0000313|EMBL:PVE11084.1, ECO:0000313|Proteomes:UP000245992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB72 {ECO:0000313|EMBL:PVE11084.1,
RC ECO:0000313|Proteomes:UP000245992};
RA Olson J.B.;
RT "Annotated genome of Streptomyces scopuliridis.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043700};
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004813}.
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:PVE11084.1}.
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; AZSP01000152; PVE11084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7T7F1; -.
DR STRING; 1440053.GCA_000718095_06761; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000245992; Unassembled WGS sequence.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:PVE11084.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245992};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 802..995
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 127354 MW; 9D61BA293BF79FD4 CRC64;
MRPAAPVKPP AAPAPVKAKP AGEATAAPEG PEYVTLRGPS AAVAKNMNAS LEMPTATSVR
AVPVKLLFDN RIVINNHLKR ARGGKISFTH LIGYAMVQAI KAMPSMNHSY AEKDGKPTLV
KPEHINFGLA IDLVKPNGDR QLVVAGIKKA ETLNFFEFWQ AYEDIVRRAR NNKLTMDDFT
GVTVSLTNPG GLGTVHSVPR LMPGQSVIMG VGSMDYPAEF QGTSQDTLNK LGISKVMTLT
STYDHRVIQG AASGEFLRIV SQLLLGENEF YDEIFQALRI PYEPVRWLKD IDASHDEDVT
KPARVFELIH SYRVRGHVMA DTDPLDYLQR KHPDLDITEH GLTLWDLERE FAVGGFAGKS
MMKLRDILGV LRESYCRTTG IEFMHIQDPK QRKWLQDRVE RPRAKPEREE QLRILRRLNA
AEAFETFLQT KYVGQKRFSL EGGESVIPLL DAVIDSAAES RLDEVVIGMA HRGRLNVLAN
IVGKSYAQIF REFEGNLDPK SMHGSGDVKY HLGAEGTFTG LDGEQIKVSL TANPSHLEAV
DPVLEGVVRA KQDIINKGGT DFTVLPLALH GDAAFAGQGV VAETLNMSQL RGYRTGGTVH
IVINNQVGFT AAPEASRSSM YATDVARMIE APIIHVNGDD PEAVVRVGRL AFEFRQTFNK
DVVIDLICYR RRGHNEGDNP QFTNPQMVRL IDKKRSVRKL YTESLIGRGD ITLEEAEQAL
QDFQGQLEKV FAEVREATSH PGTAQVPDAQ AEFPVAVTTA VSQEVVKRIA ESQVNIPDTV
TVHPRLMPQM QRRAASVEDG TIDWGMGETL AIGSLLMEGT PVRLSGQDTR RGTFGQRHAV
LVDQGTGEDY TPLQYLTDEQ ARYNVYDSLL SEYAAMGFEY GYSLARPDAL VMWEAQFGDF
VNGAQTVVDE FISSAEQKWG QTSGVTLLLP HGYEGQGPDH SSARPERFLQ MCAQNNMTVA
MPTLPSNYFH LLRWQVHNPH HKPLVVFTPK SMLRLKAAAS KAEEFTTGGF RPVIGDTSVD
PNAVRKVVFT AGKVYYDLDA ERQKRGVTDT AILRLERLYP LPGAELQAEI AKFPNAEKYL
WAQEEPANQG AWPFIALNLI DHLDLAVGAD VPHGERLRRI SRPHSSSPAV GSAKRHQAEQ
QQLVNEVFDA
//
