ID Q0SBI2_RHOJR Unreviewed; 740 AA.
AC Q0SBI2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN OrderedLocusNames=RHA1_ro03301 {ECO:0000313|EMBL:ABG95104.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG95104.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG95104.1; -; Genomic_DNA.
DR RefSeq; WP_011595950.1; NC_008268.1.
DR AlphaFoldDB; Q0SBI2; -.
DR KEGG; rha:RHA1_ro03301; -.
DR PATRIC; fig|101510.16.peg.3326; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_11; -.
DR OrthoDB; 4009369at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABG95104.1}; Pyruvate {ECO:0000313|EMBL:ABG95104.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 402..583
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 740 AA; 78783 MW; EA5B54FB0FEE02E8 CRC64;
MAEQIDDYFT SVVSGLVPVE SRPGVGPEDP IQPPSPLSVQ GALDLFDAQV GSRHLDLAAR
WLRSRGKGFY TIGSSGHEGN AAVAAALRPT DPALLHYRSG GFFLARAQQV DGSDPLRDVL
LGLVAATEEP ISGGRHKVFG RHDLNIIPQT STIASHLPRA VGVAFSIARS EKVHVPSPWP
ADAIAVGSFG DASANHSTAV GAINTAVHAA YQGLPLPLLL VCEDNGIGIS TKTPKGWIAA
NFGDRAGLEY FEADGSDLPA AYATAVSAAE WVRRNRKPAF LHLRTIRLMG HAGSDVEAAY
RTSAEITADF ERDPVLCTAK LLIERGHLSP TEILDLYEKK RAEVLELAEQ VGELPQLDSP
AAVMKPLTDS AEQAAAAAPE RVDPDRRAQF VGSPLPEDEG PLTTALAINR ALLDVLARYP
EALVFGEDVA RKGGVYGVTR GLMKKAGSAR VFDTLLDEQA ILGLALGAGV SGLLPIPEIQ
YLAYLHNAAD QIRGEGATLQ FFSDRQYRNP MVVRVAGYGY QKGFGGHFHN DNAVAALRDI
PGIVVASPAR PDDAAAMMHT CVAAARTAGA VCVYLEPIAL YHTRDLYENG DEQWLAPYPD
PAKRAGNHVP IGSARTYGDG ADLTIVTFGN GVRMSLRVAR RLERANIAAR VVDMRWLAPL
PVHDILREAN ATGRVLVVDE TRKSGGVSEG VVTALIDDGF TGPLARVTSD DSFIPLGDAA
LEVLLSEETI EAAAVKLVSR
//
