ID A0A1I4JT17_9ACTN Unreviewed; 1259 AA.
AC A0A1I4JT17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:SFL69383.1};
GN ORFNames=SAMN04488085_115118 {ECO:0000313|EMBL:SFL69383.1};
OS Geodermatophilus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=504800 {ECO:0000313|EMBL:SFL69383.1, ECO:0000313|Proteomes:UP000199152};
RN [1] {ECO:0000313|EMBL:SFL69383.1, ECO:0000313|Proteomes:UP000199152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45317 {ECO:0000313|EMBL:SFL69383.1,
RC ECO:0000313|Proteomes:UP000199152};
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; FOSW01000015; SFL69383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4JT17; -.
DR STRING; 504800.SAMN04488085_115118; -.
DR InParanoid; A0A1I4JT17; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000199152; 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:UP000199152};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 914..1107
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 37..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 137011 MW; 8AF1E3B2412AF55C CRC64;
MAGFGTNEWL VEEMYQQYLT DPSSVDQAWH EFFADYRPGS PVAASDDRER PAASPDGQAA
AAQPAAAPAP GQQPRPAAPA PQRTAGQPDG DGGSSARATP VPPRTEATVV DHAADTTATR
QKPAPAPKPA AKPAAKPAGG EGPKQTPLRG AAAAIVKNMN ASLTVPTATS VRAVPAKLLA
DNRIVINNHL ARARGGKVSF THLIGYALVR ALDDFPEMNA SYAEVDGKPV LVQPEHVNFG
LAIDLPKADG SRSLVVASIK AAEEMDFAQF WAAYEDIIRR ARAGKLTVED YSGTTISLTN
PGTIGTNHSV PRLTAGQGAI IGVGAMEYPA EFQGMSPEAL TEMAVSKIIT LTSTYDHRII
QGAQSGDFLR RLHSLLLGED GFYDGVFRSL RLPYEPVRWV PDVRVSREGQ IDKEARVIEV
IEAYRRNGHL MADTDPLEFK VRSHPDLDIL QHGLTLWDLD RTFPVGGFAG ERTMALRDIL
GVLRNSYCRT VGVEYMHITD PEERQWIQQR VELKHEQPDR EKQKHVLGRL NAAEAFETFL
QTKYVGQKRF SLEGGESVIP LLDEVLIAGT DYDLDEIAIG MAHRGRLNVL ANVLGKSYAK
IFGEFEGNID PGTVQGSGDV KYHLGAEGTF QNPFDDGKSI AVSLASNPSH LETVNPVLEG
ITRAKQDMIN KGEQGFTVMP VLLHGDSAFA GQGVVAETLN LSQLRGYRTG GTVHVVINNQ
VGFTTSPAAA RSSLYSTDVA RMIGAPVFHV NGDDPEAVVR MARLAVDYRQ AFKKDVVIDL
VCYRRRGHNE GDDPSMTQPQ MYDIIDRKRS VRKLYTEALI GRGDITLAEA EEALKDYRGQ
LERAFAETHD AQETSTPEPV MDQPQEAPVA TAISTEVLKA IGDAHVSLPQ DFTVHPKLQR
MLERRAAMVS EGGVDWAMGE LLAFGSLLMQ GVPVRLAGQD SRRGTFVQRH SVLIDRETGA
EYTPLAHLSE DQAKFFVYDS LLSEYAALGF EYGYSLADPK ALVLWEAQFG DFVDGAQMVI
DEFISSGEAK WGQRSGVVLL LPHGLEGQGP DHSSGRPERF LQLCAENNMT VANCTTPGNY
FHLLRRQALS EVHRPLVVFT PKSLLRAKAA VSPVSDFTDE TFRPVLLDPG VGGEPLEGAA
VRRVLLCSGK VAYDLLAARE AEGRADTAVL RVEQLYPLPA EQIRQALEGY PNASDVVWVQ
EEPANMGAWQ FMAVNLPEHL PAGRSLRRVS RKASASPAVG SAKVHEAEQK QLVAQAFAD
//
