ID A0A2P2GQW7_9ACTN Unreviewed; 1165 AA.
AC A0A2P2GQW7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE Flags: Fragment;
GN Name=kgd {ECO:0000313|EMBL:KKZ73902.1};
GN ORFNames=VO63_09760 {ECO:0000313|EMBL:KKZ73902.1};
OS Streptomyces showdoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68268 {ECO:0000313|EMBL:KKZ73902.1, ECO:0000313|Proteomes:UP000265325};
RN [1] {ECO:0000313|EMBL:KKZ73902.1, ECO:0000313|Proteomes:UP000265325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15227 {ECO:0000313|EMBL:KKZ73902.1,
RC ECO:0000313|Proteomes:UP000265325};
RA Thapa K.K., Metsa-Ketela M.;
RT "Draft Genome assembly of Streptomyces showdoensis.";
RL Submitted (MAY-2015) 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:KKZ73902.1}.
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DR EMBL; LAQS01000012; KKZ73902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2GQW7; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000265325; 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:KKZ73902.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265325};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 817..1010
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..22
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKZ73902.1"
SQ SEQUENCE 1165 AA; 128252 MW; 908E1F9C26C2A76E CRC64;
TVPAPAPAPA KPAAAPVAPA AAPAKPAAAA PAPVKAKEAT EAPAGPELVT LRGPAAAVAK
NMNASLEMPT ATSVRAVPVK LLFDNRIVIN NHLKRARGGK ISFTHLIGYA MVQAIKAMPA
MNHSFAEKDG KPTLVKPEHV NFGLAIDLVK PNGDRQLVVA GIKKAETLNF FEFWQAYEDI
VKRARVGKLT MEDFTGVTVS LTNPGGLGTV HSVPRLMPGQ SVIMGVGSMD YPAEFQGTSQ
DTLNKLGISK VMTLTSTYDH RVIQGAASGE FLRIVANLLL GEDGFYDDVF KSLRIPYEPV
RWLKDIDASH DDDVTKAARV FELIHSYRVR GHVMADTDPL EYKQRKHPDL DITEHGLTLW
DLEREFAVGG FAGKSMMKLR DILGVLRDSY CRTTGIEFMH IQDPKQRKWI QDRVERPHAR
VEREEQLRIL RRLNSAEAFE TFLQTKYVGQ KRFSLEGGES VIPLLDAVID SAAESRLDEV
VIGMAHRGRL NVLANIVGKS YAQIFREFEG NLDPKSMHGS GDVKYHLGAQ GTFTGLDGEQ
IKVSLVANPS HLEAVDPVVE GVVRAKQDVI NKGGTDFTVL PVALHGDAAF AGQGVVAETL
NMSQLRGYRT GGTVHIVINN QVGFTAAPES SRSSMYATDV ARMIEAPIFH VNGDDPEAVV
RVARLAFEFR QTFNKDVVID LICYRRRGHN EGDNPQFTNP QMYTLIDKKR SVRKLYTESL
IGRGDITLEE AEQALQDFQG QLEKVFAEVR EATAAPASPQ VPDARPEFPV AVTTAVSAEV
VKRIAESQVN IPERITVHPR LLPQMQRRAA SIDDGTIDWG FGETLAIGSL LMEGTPVRLS
GQDSRRGTFG QRHAVLVDQE TGEDYTPLLY LAEDQAHYNV YDSLLSEYAA MGFEYGYSLE
RPDSLVIWEA QFGDFVNGAQ TVVDEFISSA EQKWGQTSGV TLLLPHGYEG QGPDHSSARP
ERFLQMCAQD NMTVAMPTLP SNYFHLLRWQ VHNPHHKPLI VFTPKSMLRL KAAASKVEEF
TTGGFRPVIG DETVNPADVR KVVFCAGKVY YDLEAERQKR GDTETAIIRL ERLYPLPGAE
LQAEIAKYPN AAKYIWAQEE PANQGAWPFI ALNLIDHLDL AVGADIPAGE RLRRISRPHS
SSPAVGSAKR HQAEQAQLVS EVFDA
//