ID   C6WIY1_ACTMD            Unreviewed;      1242 AA.
AC   C6WIY1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   08-OCT-2025, entry version 81.
DE   SubName: Full=2-oxoglutarate dehydrogenase, E1 subunit {ECO:0000313|EMBL:ACU40057.1};
GN   OrderedLocusNames=Amir_6253 {ECO:0000313|EMBL:ACU40057.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU40057.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU40057.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00052761};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00051911};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001630; ACU40057.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6WIY1; -.
DR   STRING; 446462.Amir_6253; -.
DR   KEGG; ami:Amir_6253; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   OrthoDB; 9759785at2; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
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   FunFam; 3.40.50.11610:FF:000002; 2-oxoglutarate dehydrogenase E1 component; 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; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          902..1095
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          43..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          812..839
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        50..89
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..125
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1242 AA;  136304 MW;  7E44297B5661761F CRC64;
     MSSSPASQFG PNEWLVEEMY EQFLADPSSV DPAWHDFFAD YKSTQRNGST TTAAPTAATQ
     ADTGKAASSG APAAAKQAAS TAPAAKTPAA PAPSSAPKPK AAAPAKPAAA PAAKPAPAQA
     AKAAPVQQAK GPEQKQLRGA AAAIAKNMEL SLTVPTATSV RAVPAKLLAD NRIVINNHLK
     RTRGGKVSFT HLIGYAVVRA LQAFPNMNRH YAEINNKPHV VTPEHVNFGL AIDLPGKDGS
     RTLVVASVKG CENMTFTQFW QAYEDLIRKA RGGSLTAEDF SGTTISLTNP GTIGTNHSVP
     RLTAGQGTIV GVGAMEYPAH FQGTSEQALT DMGVSKIITL TSTYDHRIIQ GAESGEFLKR
     VHQLLLGEDG FYDDVFTSLR LPYEPIRWVA DIPEGAVDKT ARVIELIDAY RTRGHLMADT
     DPLNYRQRKH QDLDVLSHGL TLWDLDREFP VGGFAGKERM RLRDILGVLR NSYCRTVGVE
     YMHILDPEER LWIQERVEVP HEKPPATVQK YILSKLNAAE AFETFLQTKY VGQKRFSLEG
     GETVIPLLDA VLDKAAEHEL DEVVIGMPHR GRLNVLANIV GKPISQIFRE FEGNLDPGQA
     HGSGDVKYHL GAEGKYFRMF GDGETKVSLT ANPSHLEAVD PVLEGIVRAK QDILDMGGES
     FPVLPVAMHG DAAFAGQGVV AETLNLALVR GYRTGGTVHV IVNNQVGFTT APENSRSSKY
     STDVAKMIGA PVFHVNGDDP EACYWVAKLA VDYRQAFNKD VVIDMVCYRR RGHNEGDDPS
     MTQPAMYDVI DTKRSVRKTY TEALIGRGDI SVEEAEKALQ DFSSQLEHVF NEVRELEKHP
     IKASPSVEEE QQVPAKLPTG VPREVLERIA DAHVELPEGF TPHPRVKPVL ERRAKMAREG
     GIDWAYAELL AFGSLVHEGR TVRLAGQDSR RGTFTQRHAT LIDRKTGQEY TPIQNLADDQ
     GKFMVYDSVL SEFAALGFEY GYSVANPDAL VLWEAQFGDF VNGAQPIIDE FISSGEAKWG
     QVSDVVLLLP HGHEGQGPDH TSGRIERFLQ LCAEGSMTIA VPSTPANYFH LLRRHALDGV
     NRPLVVFTPK SMLRLKAAVS PVEDFVEERF KSVIDDAAIE DNSAVTKVLL CSGKIYYELV
     AEREKRGAKD TAIVRVEQLY PVPKRKLNEA LEAYPNANDV RWVQEEPANQ GAWTFYGLHL
     PELLPERYRL TRVSRRRMAA PSAGSSKVHE VEQREIITKA FE
//