ID A0A3A3Z898_9ACTN Unreviewed; 1267 AA.
AC A0A3A3Z898;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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:RJK98127.1};
GN ORFNames=D5H78_04175 {ECO:0000313|EMBL:RJK98127.1};
OS Vallicoccus soli.
OC Bacteria; Actinomycetota; Actinomycetes; Motilibacterales; Vallicoccaceae;
OC Vallicoccus.
OX NCBI_TaxID=2339232 {ECO:0000313|EMBL:RJK98127.1, ECO:0000313|Proteomes:UP000265614};
RN [1] {ECO:0000313|EMBL:RJK98127.1, ECO:0000313|Proteomes:UP000265614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 75000 {ECO:0000313|EMBL:RJK98127.1,
RC ECO:0000313|Proteomes:UP000265614};
RA Tang S., Feng Y.;
RT "YIM 75000 draft genome.";
RL Submitted (SEP-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:RJK98127.1}.
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DR EMBL; QZEZ01000001; RJK98127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3Z898; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000265614; Unassembled WGS sequence.
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 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265614};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:RJK98127.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 930..1123
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 47..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 138528 MW; 7BAF28C0DD471385 CRC64;
MSESSQSNPL AAFGPNEWLV DDLYQKYLED PESVDRAWWD FFADYAGAQG EGNGRAPQAP
QQAQQAAPQQ PAPPQPAPPQ PQQPQQAQPA PAPQAQQQPQ APQQPQAPQQ PQAQQPAARL
GAQPAPTATS PVPAAPARRP APAPAADGAE PTTRVLRGPA ARVVTNMEAS LSVPTATSVR
AVPAKLLVDN RVVINNHLKR GRGGKVSFTH LIGFAVVRAL QAMPEMNDGF TEVDGKPAVV
RPAHVNFGLA IDLAKPDGTR QLLVPSIKAA ETMDFAQFWA AYEDVVRRAR GGKLTADDFA
GTTISLTNPG TIGTNHSVPR LVKGQGTIIG VGAMEYPAEY QGASPETLAR LAVSKILTLT
STYDHRIIQG AQSGDFLRRV HQLLLGEDGF YDDVFHALRI PYEPVRWVQD LSFSHEDDVN
KTARVQELIH AYRVRGHLMA DTDPLEFQQR SHPDLDVVSH GLTLWDLDRE FPTGGFGGRP
LMKLRDILGV LRDSYCRTIG VEYMHIQEPD ERRWVQDRIE VGYAKASREE QLRILRRLNA
AEAFETFLQT KYVGQKRFSL EGGESVIPLL DAVLSEAARA GLDEACIGMP HRGRLNVLAN
IAGKSYGQIF REFEGNQDPR SVQGSGDVKY HLGTEGTFTA PSGEDVKVYL AANPSHLEAV
DPVLEGIVRA KQDKLNKGGG DGGYTVLPVL LHGDAAFAGQ GVVAETLNLS QLRGYRTGGT
IHVVVNNQVG FTTSPTSSRS SHYSTDVARM IQAPIFHVNG DDPEACVRVA RLAFEYRQAF
KKDVVIDMVC YRRRGHNEGD DPSMTQPLMY ALIEAKRSVR KLYTEGLIGR GDITVEEAEQ
ALRDYQGQLE RVFVETRGDQ GDAGDGTGLE PPSEQRGLES GPTAVASAVP LEVVKRVSDA
HVSVPEGFTV HPKLQPLLQK RAAMAGEGGI DWAMGELYAF GSLLVEGVPV RLAGQDSRRG
TFVQRHAVLT DRATGAEWTP LRNLTEDQAR FWIYDSLLSE FAALGFEYGY SVARPDALVL
WEAQFGDFVN GGQTIIDEFI STSEQKWGQR SSVVLLLPHG YEGQGPDHSS GRIERFLQMC
AEDNMTVAHP STPASYFHLL RWQAHRRERR PLVVFTPKSM LRLRAAASSV DELTSGCFRP
VIRDEQVDAA GVQRVVLCAG KVYWDLLAER TRRGDATTAL VRVEQLAPLP ADEIAEAVAP
YGDAELVWVQ EEPANQGAYP FMALNLPEAL GRPLRRVSRP ASASPAVGSH KAHDAEQRAL
VEQAFAR
//
