ID   Q5NYB8_AROAE            Unreviewed;       942 AA.
AC   Q5NYB8;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
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:CAI09946.1};
GN   ORFNames=ebA6685 {ECO:0000313|EMBL:CAI09946.1};
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI09946.1, ECO:0000313|Proteomes:UP000006552};
RN   [1] {ECO:0000313|EMBL:CAI09946.1, ECO:0000313|Proteomes:UP000006552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1 {ECO:0000313|EMBL:CAI09946.1,
RC   ECO:0000313|Proteomes:UP000006552};
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(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};
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DR   EMBL; CR555306; CAI09946.1; -; Genomic_DNA.
DR   RefSeq; WP_011239597.1; NC_006513.1.
DR   AlphaFoldDB; Q5NYB8; -.
DR   STRING; 76114.ebA6685; -.
DR   KEGG; eba:ebA6685; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000006552; 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; 1.
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:CAI09946.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006552};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          592..789
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   942 AA;  105173 MW;  BABFD67D35D26FBB CRC64;
     MMKQLRSTSY LFGANAPFIE ELYENYLADP AAVPEAWRGY FDALQAQAGA AVRDVAHGPV
     IAAFTELAKR GPVRTVTAGG DDRRQVSTLQ LINAYRFLGN RWANLDPLKR TERPQLAELE
     PSFYGFTEAD LNQSFNVGSF HGFSADHATL REILEALRQT YCGSIGSEYM HISDTGQKRW
     IQSRLESVRG TPRFSAEMKK RILERTTAAE TLEKFLHTKY VGQKRFSLEG GESTIVAMDE
     IVRVGGSLGA QEIVIGMAHR GRLNVLVNTL GKSPSMLFAE FEGKAAADLT AGDVKYHLGF
     SSDVMSPGGP VHLTLSFNPS HLEIINPVVE GSVYARQLRR KDEAKSQVIA VLIHGDAAVA
     GQGVNQEMLN FSQTRGYGTG GTVHIVVNNQ IGFTTSDPRD YRSSLYCTDI FKMVEAPIFH
     VNGDDPEAVA FATALAVEFR QEFKKDVVVD IVCYRKLGHN EQDEPMVTQP LMYRKIASHP
     GTRKLYADRL VTEGTCAPGE PEKMIKDFRE HLDKGQLLYN PVLSGHNRQY AVDWTPYIGQ
     SYTDEGETAI PLTELKRLSE RLTTLPEGFN VHPRVRKILE DRIAMGQGDL PLDWGMGENL
     AYASLLAQGF GVRISGEDVG RGTFFHRHAV LHDQKRERWD QGTYVPLKHI QDGQAALQIF
     DSVLSEEAVL AFEYGYATAE PNELVVWEAQ FGDFVNGAQV VLDQFICSGE AKWGRLCGLT
     LMLPHGYEGQ GPEHSSARIE RFMNNAAENN WQICVPTTPA QIFHLLRRQM LRKVRKPLVI
     ITPKSLLRHK EATSTLAELE DGKFRTVIGE TEALDPKKVK RVVLCQGKLY YELLAYRREN
     NIKDTALVRI EQLYPFPAAA FGAAVDQFPN AREVVWAQEE PRNQGAWYWL ASRQHLVNVL
     GSKRKLLLVS RPAAASPAVG YYAKHNAQQK AVIENAFGPL QD
//