ID A0A1Y3NTV4_9PSED Unreviewed; 943 AA.
AC A0A1Y3NTV4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=AUC60_25450 {ECO:0000313|EMBL:OUM71058.1};
OS Pseudomonas caspiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1451454 {ECO:0000313|EMBL:OUM71058.1, ECO:0000313|Proteomes:UP000195440};
RN [1] {ECO:0000313|EMBL:OUM71058.1, ECO:0000313|Proteomes:UP000195440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBF102 {ECO:0000313|EMBL:OUM71058.1,
RC ECO:0000313|Proteomes:UP000195440};
RX PubMed=28552245; DOI=10.1016/j.syapm.2017.04.002;
RA Busquets A., Gomila M., Beiki F., Mulet M., Rahimian H., Garcia-Valdes E.,
RA Lalucat J.;
RT "Pseudomonas caspiana sp. nov., a citrus pathogen in the Pseudomonas
RT syringae phylogenetic group.";
RL Syst. Appl. Microbiol. 40:266-273(2017).
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:OUM71058.1}.
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DR EMBL; LOHF01000035; OUM71058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3NTV4; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000195440; 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; 106270 MW; 5FD93C9766C8E8BB CRC64;
MQESVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGNSATDVSH
STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AQLDPLGLWQ
RTAPADLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI QDALHKTYCR TIGAEFTHIV
DSEQRNWFMQ RLESVRGRPA FSAEIQSHLL ERVTAAEGLE KYLGTKYPGT KRFGLEGGES
LIPMLDELIQ RSGSYGTKEI VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKKVELGSGD
VKYHQGFSSN VMTPGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDP NGDKVLPISL
HGDAAFAGQG VVMETFQMSQ TRGFKTGGTI HIVINNQVGF TISNPLDSRS TEYATDVAKM
IQAPILHVNG DDPEAVVFVT QLAIDYRMQF KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY
QQITKQRTTR ELYAESLIKA GVLDDARVQA KIDDYRNALD NGLHVVKSLV KEPNKELFVD
WRPYLGHAWT ARHDTRFDLK TLQELSAKLM ELPEGFVVQR QVQKIYEDRQ KMQAGGLPIN
WGYAETMAYA TLAFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDAGTYIPL QNLYAGQPRF
DLYDSFLSEE AVLAFEYGYS TTQPDALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
GLTMLLPHGY EGQGPEHSSA RLERYLQGCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
LIVLTPKSLL RHKLAVSTLE DLAEGSFQTV IPEIDTLDAA KVTRLVLCGG KVYYDLLEKR
RAEGREDIAI VRIEQLYPFP EDDLMEAIAP YTNLQKVVWC QEEPMNQGAW YSSQHHLRRS
VGNHNRNLVL EYAGRDASAA PACGYASMHA EQQEKLLQDA FTV
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