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Database: UniProt
Entry: A0A239E2D0_9ACTN
LinkDB: A0A239E2D0_9ACTN
Original site: A0A239E2D0_9ACTN 
ID   A0A239E2D0_9ACTN        Unreviewed;       708 AA.
AC   A0A239E2D0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN   ORFNames=SAMN06265355_11629 {ECO:0000313|EMBL:SNS38024.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS38024.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNS38024.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS38024.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FZNP01000016; SNS38024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239E2D0; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000198420; 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   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   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          375..556
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   708 AA;  74612 MW;  FF5FC6D9B9B4D6DD CRC64;
     MPEPADVHFL ETAATLVPSG APAPPGGLTG ERCLELFDAQ LGSRHLDLAA RRLRAQGHGF
     YTIGSSGHEG NAAVAGALRP DDPALLHYRS GAFFLERARQ VPGRNPLRDV LLGLVAAAEE
     PIAGGRHKVF GSRPLNVIPQ TSTIASHLPR ALGVAFAIER AARLGLDSPW PRDAITVCSF
     GDASANHSTA TGAVNAAVNC GHQGLPLPLL LVCEDNGIGI SVRTAPGWIH AAYGSRPGLA
     YFHADGCDLA DAHAVAARAA DWVRERRRPA FLHLRTVRLM GHAGSDVESS YRSPAEIASD
     LDRDPLLRTA RLLVDRGVAT AKDIVGRYEA KRAEVMALAE QVAGAPRLAS AAEVMAPLRY
     DAPGGGARSA EGEPVTLAQA INRTLGDLLD ERPGMLVFGE DVARKGGVYG VTRGLVRRAG
     AARVFDTILD EQSVLGLALG FGTAGMLPVP EVQYLAYLHN AADQLRGEAA TLPFFSSGRY
     RNPMVVRIAA YAYQKGFGGH FHNDNSVAAL RDIPGLVIAS PSRPDDAAGM LRACADAAGG
     EGRVCAMLEP IALYHARDLH EDGDGGWLAP AGGTVPIGRA RTYGDGGDLT VVTFANGLRM
     SLRAARRLEA AGVRCRVVDL RWLAPLPVED LLREARATGA VLVADETRRT GGVSEGVLTA
     LADAGFRGRA ARVTSEDSFI PLGDAAYHVL LSEAAIEEAA RRLLTSPR
//
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