ID   Q5FSJ1_GLUOX            Unreviewed;       885 AA.
AC   Q5FSJ1;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   OrderedLocusNames=GOX0882 {ECO:0000313|EMBL:AAW60655.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60655.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW60655.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW60655.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP000009; AAW60655.1; -; Genomic_DNA.
DR   RefSeq; WP_011252451.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FSJ1; -.
DR   STRING; 290633.GOX0882; -.
DR   KEGG; gox:GOX0882; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   Proteomes; UP000006375; Chromosome.
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:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
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; 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; 2.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAW60655.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          542..735
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          465..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  98362 MW;  451C9F5B1B8BB6BC CRC64;
     MGDHHDDRGA INGENTVYLA ELHTRWQHDP ASVDPAFASL FETLGSDRLT GADTADQSDA
     SAESLKFAYR LRGHSIAALD PLGLAPTPNI PELTPPGADR DLIARLRRAY CGTTAAEFMH
     LQDPAQRQWW IDRLENPAPG PSLDPKRILL ALTRAEGFEQ FCQKRFMGMR RFGLEGGESV
     IVALRTLIDA AAQDDIRSVS LGMPHRGRLN VMANILRKPF AAIFSEFAGA SFKPDTIEGS
     GDVKYHLGTA TTLEHAGHTV RISLLPNPSH LEAVDPVVLG RVRADQDREK DRERQHHLGI
     LVHGDAAFAG QGVVYETLSL SKLEGYRTGG TVHVIINNQI GFTTVQSDAH SGLHNTDIAK
     SVQAPILHVN GDDPEAVSRC AFLAHEWRRT FQSDIVLDVV CYRRHGHNEA DEPAFTQPAM
     VHAIQSRATT RSLYADHLIR TGVMTEAEVE EMWAHFQRRL EEQFEKSKTY QPDGTDWLDG
     PEDPTRLQDE QDRIQPMTGV PLRRLQEVGE AIGTIPEGLA VHPRLTRQII ARGKAVADGG
     PIDWATAEAL AFGTLSMDGH PVRLSGQDSR RGTFSQRHAV LFDQDTGRED TPLTHIAPHQ
     APLNIWNSPL SEYAVLGFEY GYSLGDPEAL VLWEAQFGDF ANGAQIILDQ FIASGETKWL
     RTSGLTLLLP HGYEGGGPEH SSARPERILQ LCAENNMRVC DITTPANYFH ALRRQIARRC
     RKPLVVFTPK SLLRNKDAVS MLDEMGPHTR FQPVIADPAK EDGARRIILC TGKVYYDLAA
     ERTRQNRDDV AIIRVEQLYP FPHHALMEQL ARHPEAEQVL WCQEEPQNNG AWIFVDRRIE
     RALRGCNHRV QRPDYVGRES AASPATGLPG VHAAQQEKLV QDALS
//