ID   B1XV04_POLNS            Unreviewed;       956 AA.
AC   B1XV04;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Pnec_0998 {ECO:0000313|EMBL:ACB44181.1};
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB44181.1};
RN   [1] {ECO:0000313|EMBL:ACB44181.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1 {ECO:0000313|EMBL:ACB44181.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT   "Complete sequence of Polynucleobacter necessarius STIR1.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001010; ACB44181.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1XV04; -.
DR   STRING; 452638.Pnec_0998; -.
DR   KEGG; pne:Pnec_0998; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   OrthoDB; 9759785at2; -.
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:ACB44181.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          602..799
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   956 AA;  107015 MW;  A8A652B3B260A414 CRC64;
     MKDEHIMQDQ RDNSYLLGGN APYVEELYES YLHDPASVAD HWRDYFDNVK QVPAVDGSSR
     TDIAHGPIVA SFAERAKQGP IRTISDSADS EMGRKRVAVQ QLIAAYRNVG NRWANLDPLK
     RTERQDIPEL DPAFYDFTDG DMDIVFNTSN TFFGKNEMSL RDLLQALRET YCGTIGVEFM
     FIADQKIKKW WQEKLESIRS TPQFNVDEKR QILDRVTAAE GLERYLQAKY VGQKRFSLEG
     GESFIACMDE LIRDAGNKGV QEIVIGMAHR GRLNVLVNTL GKMPKDLFAE FEHKGPETLP
     AGDVKYHQGF SSDISTSGGP VHLSLAFNPS HLEIVNPVVE GSARARMERR GDMLGEQVMP
     VLVHGDAAIA GQGVMQETLA MSEVRGYSTG GTMHIVINNQ IGFTTSDPRD LRSSLYCTDI
     MKVVDAPVLH VNGDDPEAVV LATKLAVEFR MKFHKDVAID IICFRKLGHN EQDTPAMTQP
     LMYKIIAAHP GTRKLYADKL ETQGVLPAGT GDLMVKEYRA AMDEGKQTSD LVLSNFKGKF
     AVDWSPFLNK KWTDEADTAT PLTEWKRLAE KISTIPEGFK AHPLVSKVYN DRAAMGRGEV
     NIDWGMGEHM AFASLVASGY PVRLSGEDSG RGTFTHRHAV LHEQNREKWD TGTYIALQHV
     TKDQAPFVVI DSILSEEAVL GFEYGYAAAE PNTLTIWEAQ FGDFVNGAQV VIDQFIASGE
     VKWGRANGLV MMLPHGYEGQ GPEHSSARLE RFMQLCADTN MQVIQPTTAS QIFHVLRRQM
     IRQFRKPLIL MTPKSLLRNK EAASPLSEFT KGGFQTVIGE RDESIDAKQV TRLVMCSGKV
     YYDLVKQRAE KKIGDVVIIR LEQLYPFPHK ALTAELKKYP KLEEVIWCQD EPQNQGAWFF
     VQHNILENMS DGMKLGYAGR PASASPACGY AHLHQEQQKS LLNAAFAKLK GYVITK
//