ID A0A285HEA1_9ACTN Unreviewed; 750 AA.
AC A0A285HEA1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=SAMN05421748_104224 {ECO:0000313|EMBL:SNY34055.1};
OS Actinoplanes atraurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY34055.1, ECO:0000313|Proteomes:UP000219612};
RN [1] {ECO:0000313|EMBL:SNY34055.1, ECO:0000313|Proteomes:UP000219612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY34055.1,
RC ECO:0000313|Proteomes:UP000219612};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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:ARBA00043693};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; OBDY01000004; SNY34055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285HEA1; -.
DR OrthoDB; 4009369at2; -.
DR Proteomes; UP000219612; Unassembled WGS sequence.
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; -; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219612}.
FT DOMAIN 410..591
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 750 AA; 78827 MW; 793F23AEC472EA4E CRC64;
MAGLARLRDA GRVTTPQNLD ERFRDAVSAL PLPGDRRAPG DPVRDGSTLT GARALELFDA
QLASRHLDLA ARWLRSFNEG FYTIGSSGHE GNAAVAAALL PTDPALLHYR SAAFFSARAK
SLVDAARDVL RGVVASAREP IAGGRHKVFG SAELNIIPTT STVASHLPRA VGLAFSQGRS
SRDAIVAASF GDASINHATA TAALNAAGWF EHSSVPLPLL LICEDNGLGI SVPSPDGWVA
AMLGSRPGLR YTAADGCDLA GTYDAATDAA GYVRRERRPA VLHLSTVRLM GHAGADAEVG
YRPAEEIRRD LERDPLVATA RMLVTAGLMT PDEAITRYDE VGWQVRKVAE EVLGDPKLTT
VAEIVAPLAP RRPLRSAHAI TEAASRALGP GASARSRVFG GKLPENAGPL TLAQTVNAAL
TDALAADPGV LVFGEDVGRK GGVYGVTKHL QERFGAERVF DTLLDETTIL GLALGAGLDG
MLPIPEIQYL AYLHNAEDQL RGEAATMSFF SSGAYKNPMV VRVAGLAYQQ AFGGHFHNDN
SVAVLRDVPG LVLAVPARAA DAAPMLRSCL ASAAADGSVC VFLEPIALYH TRDLHEQGDG
EWLAPYAGPH AWSSEHVPIG RARTYAVGNA ADLTIITYGN GLRMSLRVAS RLAEQGYGSR
VVDLRWISPL PVNDLVREAA ATGRVLIVDE TRRSGGVGEG VLAALVDGGF VGSARRIASA
DSLIPLGPAA QQVLVGEDAI TQGAHTLLAR
//
