ID   D5UBM6_CELFN            Unreviewed;      1250 AA.
AC   D5UBM6;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=2-oxoglutarate dehydrogenase, E1 subunit {ECO:0000313|EMBL:ADG74121.1};
GN   OrderedLocusNames=Cfla_1219 {ECO:0000313|EMBL:ADG74121.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS   18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74121.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG74121.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC   NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688; DOI=10.4056/sigs.1012662;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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   -!- 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=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; CP001964; ADG74121.1; -; Genomic_DNA.
DR   RefSeq; WP_013116455.1; NC_014151.1.
DR   AlphaFoldDB; D5UBM6; -.
DR   STRING; 446466.Cfla_1219; -.
DR   KEGG; cfl:Cfla_1219; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   OrthoDB; 9759785at2; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000000849; Chromosome.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000849};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          911..1104
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          50..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1224..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          804..831
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        84..100
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1250 AA;  137263 MW;  2874875682026E20 CRC64;
     MTQNAQSDST RADFGANEWL VDELYEQYLK DRNAVDPAWW DFFEGYKPET TGAATNGETK
     DAPRATAAPP APAQPTTART PAAPAVPAAP PAPPVEVTPS PVATAQPATA PYAEAATRRT
     DAPEVQAVDD VQKLRGPAAR VVTNMEASLE VPTATSVRAV PAKLMVDNRI VINNHLSRGR
     GGKVSFTHLI GFALVEAVQE MPAMNAAYTL VDGKPGVLQP AHVNLGLAID LAKPDGSRQL
     LVPSIKKAET LDFAQFWTAY EDVVRRARNS KLTVDDFAGT TISLTNPGTI GTVHSVPRLM
     QGQGTIVGVG AMDYPAEFAG TSDEQLNRMG VSKVLTVTST YDHRIIQGAQ SGDFLRILGR
     KLLGEDGFYD RVFAALRVPY EPVRWVRDAN HDPDAEAIKP ARVAELIHAY RSRGHLMAET
     DPLAYRQRKH PDLDVQNHGL TLWDLDRTFP TGGFTGRTRA TLREVLGLLR DSYCRTVGVE
     YMHLQDPRQR RWLQERLESG YARTPREDQL RILRRLNAAE AFETFLQTKF VGQKRFSLEG
     GESLIPLLDA ILSRAADGGL DEVGIGMAHR GRLNVLANIA GKSYGQIFSE FEGNQDPKSV
     QGSGDVKYHL GTEGVFTAES GATTAVYLAA NPSHLEAVDP VLEGIVRAKQ DRIDLGGDGF
     SVLPILIHGD AAFAGQGVVF ETLNLAQLRG YRTGGTIHVI VNNQVGFTTG PSSSRSSQYA
     TDVAKGLQVP IFHVNGDDPE AVVRVAELAF EYREQFDRDV IIDMVCYRRR GHNEGDDPSM
     TQPLMYNLIE AKRSVRKLYT ETLVARGDIT LEEAEQALRD YQSQLERVFT ETREDGWTPP
     PADVETVAGL ERPESQQEDA GVMVGWQTAV PTSILQRIGQ AHVSPPEGFT VHPKLAQMLA
     KREQMSREGG IDWGFGEILA FGSLLIEGTP VRLAGQDSRR GTFVQRHAVL HDRETGAEWT
     PLLYLSGDQA KFWVYDSSLS EYAALGFEYG YSVERPDALV LWEAQFGDFV NGAQTVIDEF
     ISSAEQKWAQ RSSVVLLLPH GYEGQGPDHS SARIERFLQL AAEDNMTIAQ PSTPASHFHL
     LRRQAYQRPR RPLVVFTPKS MLRLKSASSD VQDFTSGTFR TVIGDDLAAA KADQVTRVLL
     CSGKVYWDLL AQRVAANDQQ TAIVRFEQLY PLEPDAIAEA LAPFGDAELV WVQDEPRNQG
     PWTFVSTHLP QVVGREVRVV SRPESASPAA GSAKKHAVEQ KSLVTEAFAR
//