ID A0A2U2ZTJ5_9ACTN Unreviewed; 1275 AA.
AC A0A2U2ZTJ5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit {ECO:0000313|EMBL:PWI15609.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:PWI15609.1};
GN Name=kgd {ECO:0000313|EMBL:PWI15609.1};
GN ORFNames=DI272_16600 {ECO:0000313|EMBL:PWI15609.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI15609.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI15609.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI15609.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-2018) 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:PWI15609.1}.
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DR EMBL; QFRX01000001; PWI15609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZTJ5; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000245455; 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; IPR032106; 2-oxogl_dehyd_N.
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; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:PWI15609.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245455};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:PWI15609.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 927..1120
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 838..865
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 138920 MW; EC2E1A67658418ED CRC64;
MSPQSPSNSS ISTDADQAGK NPAAAFGPNE WLVDEIYQQY LQDPNSVDRA WWDFFADYKP
GAAAAPAAPA APAAAAPAAP AAPAAPAAPA APAAPSVPAP APAAPAAAPQ PAAAAPAPAA
PAPAAAPAAA PAKPAAAKPA AKAAPAAAAA APAEGPELVT LRGPAAAVAK NMNASIEVPT
ATSVRAVPVK LLFDNRIVIN NHLKRARGGK ISFTHLIGYA MVQAIKAMPS MNYSFMEKDG
KPTLVKPEHV NFGLAIDLVK PNGDRQLVVA GIKKAETLNF FEFWQAYEDI VRRARDGKLT
MDDFSGVTVS LTNPGGLGTV HSVPRLMPGQ SVIMGVGSMD YPAEFQGTSQ DTLNKLGISK
VMTLTSTYDH RVIQGAASGE FLRIVANLLL GENGFYDDIF EALRIPYEPV RWLRDIDASH
DDDVTKAARV FELIHSYRVR GHVMADTDPL EYRQRKHPDL DITEHGLTLW DLEREFAVGG
FSGKSLMKLR DILGVLRDSY CRTTGVEFMH IQDPKQRKWI QDRIERPHTK PEREEQLRIL
RRLNAAEAFE TFLQTKYVGQ KRFSLEGGES VIPLLDAVID SAAESRLDEV VIGMAHRGRL
NVLANIVGKS YAQIFREFEG NLDPKSMHGS GDVKYHLGAE GTFTGLDGEQ IKVSLVANPS
HLEAVDPVLE GVARAKQDII NKGGTDFTVL PVALHGDAAF AGQGVVAETL NMSQLRGYRT
GGTVHIVINN QVGFTAAPES SRSSMYATDV ARMIEAPIFH VNGDDPEAVV RVARLAFEFR
QAFNKDVVID LICYRRRGHN ESDNPAFTQP LMYDLIDKKR SVRKLYTESL IGRGDITLEE
AEQALQDYQG QLEKVFTEVR EATSQPASAE SSDPQAEFPV AVNTAVSTEI VKRIAESQVN
IPDNITVHPR LLPQLQRRAA MVEDGTIDWG MGETLAVGSL LLEGVPVRLA GQDSQRGTFG
QRHAVIIDRE TGDEFTPLMY LSEEQARLNV YNSLLSEYAA MGFEYGYSLA RPESLVMWEA
QFGDFVNGAQ TVVDEFISSA EQKWGQTSGV TLLLPHGYEG QGPDHSSARP ERFLQLCAQN
NMTVAMPTLP SNYFHLLRWQ VHNPHHKPLI VFTPKSMLRL KAAASKAEEF TTGQFRPVIG
DASVDPAAVR KVVFCAGKVY YDLEAERQKR GVTDTAIIRI ERLYPLPGAE LQAEIAKYPN
AEKYLWAQEE PANQGAWPFI ALNLIDHLDL AVGADVPHGE RLRRISRPHG SSPAVGSAKR
HQAEQEQLVR EVFEA
//
