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Database: UniProt
Entry: A0A263D6A9_9PSEU
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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
//
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