ID   A0A1X0N040_9PSED        Unreviewed;       943 AA.
AC   A0A1X0N040;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=BZK31_24565 {ECO:0000313|EMBL:ORC55698.1};
OS   Pseudomonas floridensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1958950 {ECO:0000313|EMBL:ORC55698.1, ECO:0000313|Proteomes:UP000192815};
RN   [1] {ECO:0000313|Proteomes:UP000192815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEV388 {ECO:0000313|Proteomes:UP000192815};
RA   Timilsina S., Vallad G.E., Jones J.B.;
RT   "Pseudomonas floridae sp. nov., a novel pathogenic bacterial species
RT   isolated from tomato.";
RL   Submitted (FEB-2017) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORC55698.1}.
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DR   EMBL; MUIO01000112; ORC55698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0N040; -.
DR   STRING; 1958950.BZK31_24565; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000192815; Unassembled WGS sequence.
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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          599..792
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   943 AA;  106512 MW;  887DD38E82082C51 CRC64;
     MQESVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGSSATDVSH
     STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA ARLDPLGLWQ
     RPAPADLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI HEALQQTYCR TIGSEFTHIV
     DSEQRNWFMQ RLESVRGRPV FSADIQSHLL ERVTAAEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDELIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKKVELGSGD
     VKYHQGFSSN VMTAGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDP NGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFKTGGTI HIVINNQVGF TISNPLDSRS TEYATDVAKM
     IQAPILHVNG DDPEAVMFVT QLAIDYRMQF KRDIVIDLVC YRRRGHNEAD EPSGTQPLMY
     QQITKQRTTR ELYAEHLIKT GILDDARVQG KVDDYRNALD NGLHVVKSLV KEPNKELFVD
     WRPYLGHAWT ARHDTRFDLK TLQELSAKLM ELPEGFVVQR QVQKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLAFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDAGTYIPL QNLYAGQPRF
     DLYDSFLSEE AVLAFEYGYS TTEPNALVIW EAQFGDFANG AQVVVDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
     LIVLTPKSLL RHKLAVSTLE ELAEGSFQTV IPEIDTLDPA KVTRLILCSG KVYYDLLEKR
     LAEGREDIAI VRIEQLYPFP EDDLMETIAP YTNLQNVVWC QEEPMNQGAW YSSQHHLRRS
     VGNHKRELVL EYAGRDASAA PACGYASMHA EQQEKLLQDA FTV
//