ID   Q2S3D2_SALRD            Unreviewed;      1243 AA.
AC   Q2S3D2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:ABC45112.1};
GN   OrderedLocusNames=SRU_1173 {ECO:0000313|EMBL:ABC45112.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45112.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC45112.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31
RC   {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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   -!- 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; CP000159; ABC45112.1; -; Genomic_DNA.
DR   RefSeq; WP_011403927.1; NC_007677.1.
DR   RefSeq; YP_445299.1; NC_007677.1.
DR   AlphaFoldDB; Q2S3D2; -.
DR   STRING; 309807.SRU_1173; -.
DR   EnsemblBacteria; ABC45112; ABC45112; SRU_1173.
DR   GeneID; 83728082; -.
DR   KEGG; sru:SRU_1173; -.
DR   PATRIC; fig|309807.25.peg.1217; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OrthoDB; 9759785at2; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000008674; Chromosome.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:ABC45112.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          898..1091
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          40..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1216..1243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1243 AA;  138870 MW;  8369084273B3305E CRC64;
     MSSLGFNTGY IEELYKQYQD DPDSVSESWR EFFADYDPDA SFIPVDRTTA GDGEATTPPE
     EPTEPEPTDR DSSPDASSAP PAEADDGVVE PLRPASAPAV DEDQADVTAM TGPSAKVVEN
     MEDSLGIPTA TSARTIPVKL LDENRNLLND YQKQVGGEKV SYTHIIAYAM VQAMQKYPDM
     NTTFRRNEDG TPEHVKPDQI NLGLAIDVER RGERTLLVPN LKDAGSLSFA EFLGTYNNIV
     GRALGGDLDL SDFQGTTATL TNPGMIGTSM SVARLMPGQG VIMGAGAIDF PPEYRGYDSE
     VASKAGVSPV MTLTSTYDHR VIQGATSGAF LNHIEELLTG NHDFYQRIFS DLGVPYQPFR
     MATDSTPQLG RSRPQDELDM TEKQAAVLQL IRAYRVRGHL QADINPLGYE WQYHEELDPA
     TYGLTVWDLD REFITGGLGG EDKLPLREIL SILRKSYTSK VGTAFMHISD PEEKTWIQNR
     IEPMRNAGSP SEEERHRIVQ KLNAAEAFER FLHTKYIGHK RFSLEGSETM IPLIDTLLSD
     AADEGVEEVV MGMAHRGRLN VLANIIGKPY EEIFSKFEGN IDPNTTQGSG DVKYHLGAEG
     DVTSPDGNEI SVTLASNPSH LEAVNPVVEG MSRAKQNLLR DEHPEAAEDD YHDAVMPLLI
     HGDAGFAGQG VVAETLNLSK LRGYTTGGTV HLVINNQIGF TTPPGDARSS TYATDLARAI
     EAPIFHVNGD DPETCVRIAR LAFEYRQRFN KDVVIDMMCY RVHGHNEGDE PTFTQPLLYE
     KIEEKRSPRK LYTEMLLRRG EIEPDEAEQM LDDYRGRLQE AFERTKDLEE KDADEALEER
     VQRTADDRLP PVDTTAEREH LERVVEVLTD FPDDFNVHRK LERLFGKRDD LFYDEKRIDW
     AFSETLAFGS LLQEGTRVRL SGQDSRRATF SQRHAVLIDQ ETGAEYTPLN NLTDDQERLL
     IYDSLLSEYA VAGFEYGYSV VDKNALTCWE AQFGDFANGA EIVWDQFVSA AEEKWGQTSG
     LVALLPHAYE GQGPEHSSAR LERFLQLCAE QNMIVANFST PANYFHALRR QVKRDVKKPL
     IIMTPKSLLR HPKCVSTPED LMEGGVQEII PAEADPAGTM RHILCSGKVY YDLVTALEDT
     DRRDEIAITR LEQFYPFPES DLQEELERYA EADETVWVQE EPQNMGAWSF VSPRFETLLD
     EIHGPCEQRI QYVGRPASAS PATGSAKVHD REQEQLVGDA LGL
//