ID A0A1C5HSU3_9ACTN Unreviewed; 915 AA.
AC A0A1C5HSU3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=GA0070614_1735 {ECO:0000313|EMBL:SCG49052.1};
OS Micromonospora coxensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG49052.1, ECO:0000313|Proteomes:UP000198215};
RN [1] {ECO:0000313|EMBL:SCG49052.1, ECO:0000313|Proteomes:UP000198215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG49052.1,
RC ECO:0000313|Proteomes:UP000198215};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:ARBA00043693};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; LT607753; SCG49052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5HSU3; -.
DR OrthoDB; 4009369at2; -.
DR Proteomes; UP000198215; Chromosome i.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 3.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 575..756
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 118..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 94391 MW; 33D2D31CE93D1DDD CRC64;
MLIDVTTPQD LDDRFRETLG ALPEPERRRD PAEPVRAGAA LTGRHLLALF DAQVTSRQLD
LAGRWLRSFD EGYYTIGSAG HEANAAVAAA LRPTDPALLH YRSGAFYCTR AAQAAGEFPA
PRPADGTPTS GGPVAAADFD DGGTAGSGGP DDGVSGSGGP TAADGPDQSA AHDPDDAADR
TGGAPEHAAG TGPATPAVAE AGGLTGTVTA GYRVGADGTA EAVTVELPAD PPSADDAAAA
RPDAGTAPER RGEAAAEGAP GGPDDDAYAD AARDVLRGMV ASAREPIAGG RHKVFGRADL
AVVPTTSTIA SHLPRAVGLG LALERLRRVE TAGRRGGDSP LRSPWPRDAI VVCSFGDASV
NHASATAALN TAGWYDHTGL RIPVLFLCED NGLGISVRSP EGWVERALRA RPGVRYFAAD
GADPVGTYAV AAEAAAWVRR HRRPAVLHLR TVRLMGHAGA DAETAYRSTA EITADEARDP
LLATARTLVE AGMATGEELL TRYDERGWQV RRIAEEVLDE PKLGSVAEVV APLAPRRPAR
VAATVAESAA RAAGPGAAAR AEVFGGKPPE LAGPLTLAQS VNAALADAML AHPGMAVFGE
DVAAKGGVYG VTKGLREKFG AARVFDTLLD ETSVLGLGLG AGLAGMLPVP EIQYLAYLHN
AEDQLRGEAA TMQFFSQGAF RNPMVVRVPG LAYQEGFGGH FHNDNSVAVL RDVPGLVIAV
PARPDDAAPL LRTCLAAAAV DGTVSVLLEP IALYHVRDLY EPGDGEWLGQ YAEPGAWAAG
HVPIGRARVY GVGSAEDVTI LTFGNGVRMS LRAAATLADE GIGTRVVDLR WLAPLPVADI
IREASATGRV LVVDETRRSG GVGEGIIAAL VDAGYVGAAR RVAAIDSFVP LGPAARQVLV
SEEAITQGAR ALLAR
//
