ID A0A1H1ZS64_9ACTN Unreviewed; 1279 AA.
AC A0A1H1ZS64;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:SDT36548.1};
GN ORFNames=SAMN04489812_5415 {ECO:0000313|EMBL:SDT36548.1};
OS Microlunatus soli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=630515 {ECO:0000313|EMBL:SDT36548.1, ECO:0000313|Proteomes:UP000199103};
RN [1] {ECO:0000313|EMBL:SDT36548.1, ECO:0000313|Proteomes:UP000199103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21800 {ECO:0000313|EMBL:SDT36548.1,
RC ECO:0000313|Proteomes:UP000199103};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; LT629772; SDT36548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1ZS64; -.
DR STRING; 630515.SAMN04489812_5415; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000199103; Chromosome i.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
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 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199103};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 935..1128
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 139779 MW; 3E996ABE212323A9 CRC64;
MATAPDPNST STQHADEDFG ANDWFIEQMY EQYVADPKSV DASWAQFFST NGAPGSNRPA
AAPPTKPSGD ATANGKSAQS GTAAQPATKT AAPAAKSEAK ASSVTASAAK AADPAPQAAK
SAPAAKVESK TVQPSKPTTG TGLPADPPNP ADRPEVAPDK PVRTVMRGAP MRTAKNMDAS
LTVPTATSVR SLPVKLLIDQ RIVINNHLRR ARGGKVSFTH IIGYAIVQAL KAVPDMNVAY
DVTDGKPTLV KPTHINLGLA IDLPKPDGTR QLVVPSIKSA ENLDFAQFWA AYEEIVKKAR
GNKLTVDDFA GTTISLTNPG TIGTNHSVPR LMNGQGAIIG VGSMEFPAEF QGSNPNRLNS
FGVGKIMTLT STYDHRVIQG ALSGEFLAKL HGLLLGEDNF YRDIFASLRI PTAPIEWAVD
RSAVHEDEVS KQARVFELIN AYRVRGHLMA DIDPIAYHLR DHPDLDVQTH ELTLWDLDRE
FATGDFADGS GLMTLRKILG ILRDSYCRTI GLEYMHIQER EQRRWIQAHV ERPHESLPRE
EHLRILDKLN EAEVFETFLQ TKYVGQKRFS LEGGESTIAL LDEICEQAAN DHLDEVTIGM
AHRGRLNALA NIVGKSYTQI FREFEGNIDP RTVQGSGDVK YHLGAEGKFT SLAGNTIKTS
MAANPSHLEA VDGVLEGITR AKQDILDRGA EYPVLPLLVH GDAAFAGQGV VAETLALSQL
RGYRTGGTIH VVVNNQVGFT TTPGEGRSST YATDVARMVQ APIFHVNGDD PEACIRVARL
AYEFRREFNK DVVIDLVCYR SRGHNEGDDP SVTQPLMYDL ISKKRGVRKL YTEALIGRGD
ITIEDAEEVL KKFQVRLESV FEEVRQAANV PVDTEYRRVP KYPEKTGAKH GTAISSEVMQ
KIADAHLNPP EGFTVHPKVQ PQLQRRAKAI TEGGIDWATG ELLALGSVMI EGRPVRLAGQ
DTRRGTFVQR FAAVVDRKNA DVWIPLQHLS PDQGRFHVFN SPLSEYAAMG FEYGYSVARP
EALVMWEAQY GDFSNGAQTI IDEFITAGQS KWGQKSGVVL LLPHGYEGQG SDHSSARIER
WLQLAADDAF AVAQPSNSAS YFHLLRNHAL GANHKPLIVL TPKRMLRMKA AASEPADFTD
GQWQPVLGDP TITDPSTVRR VVMASGMARW DLMAERDKLG KNQEIAVVSL ERYYPLPAEQ
IAAELARYGN AESFRWVQYE PKNQGAWPFL ALNLPDALAE HGARLPLTPV TRAASSAPAT
GSHKVHEAEQ KEIYNAALG
//
