ID A0A0A1YKF3_9PSED Unreviewed; 943 AA.
AC A0A0A1YKF3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=TMS3_0116995 {ECO:0000313|EMBL:KFX69159.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX69159.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX69159.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX69159.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(2014).
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:KFX69159.1}.
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DR EMBL; AWSQ01000004; KFX69159.1; -; Genomic_DNA.
DR RefSeq; WP_025166393.1; NZ_AWSQ01000004.1.
DR AlphaFoldDB; A0A0A1YKF3; -.
DR STRING; 1395571.TMS3_0116995; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000030063; 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 Reference proteome {ECO:0000313|Proteomes:UP000030063};
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; 106489 MW; 68D36C7B9DF52A2C CRC64;
MQESVMQRMW DSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPT DGSAATDVSH
STVRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRMI QAYRMRGHQA ARLDPLGLWQ
RPVPADLSIN HYGLTDADLD TTFRTGGLYI GKEEASLREI HQALQHTYCH TIGAEFTHIV
DSEQRSWFQQ RLESVRGRPQ FSAEVQSHLL ERLTAAEGLE KYLGTKYPGT KRFGLEGGES
LIPLLDEVIQ RSGAYGTKEI VIGMAHRGRL NVLVNTFGKN PRDLFDEFEG KKTEGLSSGD
VKYHQGFSSN VMTAGGEVHL ALAFNPSHLE IVSPVVEGSV RARQDRRSDV AGEKVLPISI
HGDAAFAGQG VVMETFQMSQ TRGYKTGGTI HIVINNQVGF TTSRAEDSRS TEYCTDVAKM
IQAPIFHVNG DDPEAVLFVT QLAVDYRMQY KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
QQISKQRTTR ELYAEALTTA VSHSTDDVQF KIDEYRTALD NGQHVVKSLV KEPNKELFVD
WRPYLGHAWT ARHDTRFDLK TLQDLSNKLM EVPEGFVVQR QVAKILEDRH KMAAGALPIN
WGYAETMAYA TLLFEGHPIR MTGQDIGRGT FSHRHAALHN QKDGSTYLPL QNLYEGQPRF
DLYDSFLSEE AVLAFEYGYA TTKPNSLVIW EAQFGDFANG AQVVFDQFIS SGEHKWGRLC
GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNMQVCVPT TPAQIYHLLR RQVIRPLRKP
LVVLTPKSLL RHKLAISTLE DLAEGSFQTV IPEVDAIDAK KVDRLILCSG KVYYDLLEKR
RNEGREDIAI VRIEQLYPFP EDDLTEVLAT YKSLKHIVWC QEEPMNQGAW YCSQHHMRRV
ATAHKKTLFL EYAGREASAA PACGYASLHA EQQAKLLQDA FTV
//
