ID A0A263D6A9_9PSEU Unreviewed; 1265 AA.
AC A0A263D6A9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:OZM73729.1};
GN ORFNames=CFN78_09465 {ECO:0000313|EMBL:OZM73729.1};
OS Amycolatopsis antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM73729.1, ECO:0000313|Proteomes:UP000242444};
RN [1] {ECO:0000313|EMBL:OZM73729.1, ECO:0000313|Proteomes:UP000242444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU-G6 {ECO:0000313|EMBL:OZM73729.1,
RC ECO:0000313|Proteomes:UP000242444};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT Antarcticus brown macroalga.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001267};
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:ARBA00033664};
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:OZM73729.1}.
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DR EMBL; NKYE01000004; OZM73729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263D6A9; -.
DR InParanoid; A0A263D6A9; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000242444; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000242444};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 924..1117
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 49..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 834..861
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 138684 MW; 0591B9E69E9B1F91 CRC64;
MSSSSPASQF GPNEWLVEEM YDQFLADPSS VDAAWHDFFA DFTPTQAAKD DAGAAKDGAA
SGSPQGNGTA PSRAEQPSAS GSAKAPEKQA PAKPAPAKPA PEQQAPAKQA PVAKPAAAPA
KTASAPAPAK AQAAPAKADA KDSKDAKAPA KDAPESKQLR GAAAAIAKNM DASLTVPTAT
SVRAVPAKLI ADNRIVINNH LKRTRGGKIS FTHLIGYAMI RALREYPNMN RHYALVDGKA
HSVTPEHVNF GLAIDMKGKE GARTLVVASI KNTENMTFLQ FWQAYEDIVK KARNNKLTAD
DFSGTTISLT NPGGIGTNHS VPRLQAGQGT IIGVGAMQYP AHFEGTSEKT LVDLGVSKIM
TLTSTYDHRI IQGAESGEFL KHIHQLLLGE AGFYDDVFTS LRLPYEPVRW VQDIPEGAVD
KTARVIELID AYRMRGHLMA DTDPLNYRQR RHEDLDVLSH GLTLWDLDRE FAVGGFAGKE
RMKLRDVLGV LRNSYCRTVG IEYTHILDPD ERRWIQDRVE VPHEKPDTSV QKYVLSKLNA
AEAFETFLQT KYVGQKRFSL EGGETVIPLL DTVLDKAAEH ELDEVVIGMP HRGRLNVLAN
IVGKPIAQIF QEFEGNLDPG QAHGSGDVKY HLGAEGKYFR MFGDGETRVS LTANPSHLET
VDPVLEGIVR AKQDILDKGG EGFTVLPVLL HGDAAFAGQG VVAETLNLAL LRGYRTGGTV
HVIINNQVGF TTAPENSRSS QYATDVAKMI AAPVFHVNGD DPEAAHWVAQ LAVEYRQTFN
KDFVIDMICY RRRGHNEGDD PSMTQPAMYD IIDTKRSVRK TYTESLIGRG DISVEEAEAA
LRDFSSQLEH VFNEVRELEK HPVSASPSVE EEQQVPAQVP TAVSRDVVER IGDAFGEAPE
GFSPHPRVKP VMERRQKMSR EGGIDWAFGE LLAFGSLAIE GRLVRLSGQD SRRGTFTQRH
SVLIDRKTGQ EYQPLQNLAE EQGRVMIYDS ALSEYAAVGF EYGYSVANSE ALVMWEAQFG
DFVNGAQTII DEYISSGEAK WGQLSDVVLL LPHGHEGQGP DHTSGRIERF LQLCAEGSMT
VSVPSTPANY FHLLRRHALD GVNRPLIVFT PKRLLRDKAV KSGVEDFTSG SKFLSVIDDN
DVSPEKARKV LLTSGKMYWE LVAERTKQEI EDVAIVRVEQ YYPLPKKKLA AALERFTKAT
EIMWVQEEPE NQGAWPFFGL NLPRKFPELL AGLQVAARRP MAAPSAGSSK VHEVEQKAII
AKAFS
//