ID J2MC19_9PSED Unreviewed; 943 AA.
AC J2MC19;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=PMI18_02234 {ECO:0000313|EMBL:EJM02401.1};
OS Pseudomonas sp. GM102.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144321 {ECO:0000313|EMBL:EJM02401.1, ECO:0000313|Proteomes:UP000007514};
RN [1] {ECO:0000313|EMBL:EJM02401.1, ECO:0000313|Proteomes:UP000007514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM102 {ECO:0000313|EMBL:EJM02401.1,
RC ECO:0000313|Proteomes:UP000007514};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM02401.1}.
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DR EMBL; AKJB01000049; EJM02401.1; -; Genomic_DNA.
DR RefSeq; WP_007898987.1; NZ_AKJB01000049.1.
DR AlphaFoldDB; J2MC19; -.
DR PATRIC; fig|1144321.3.peg.2180; -.
DR Proteomes; UP000007514; 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; 106590 MW; 8FAAB63ED5E2E1EF CRC64;
MQESVMQRMW NSAYLSGSNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGNTATDVSH
STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AQLDPLGLWQ
RPAPADLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI HEALQQTYCR TIGAEFTHIT
DSEQRQWFQQ RLESVRGRPT YSVDIKSHLL ERVTAGEGLE KYLGTKYPGT KRFGLEGGES
LIPMLDELIQ RSGSYGTKEI VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKKVELGSGD
VKYHQGFSSN VMTTGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDP TGEKVLPISI
HGDAAFAGQG VVMETFQMSQ TRGFKTGGTV HIVINNQVGF TISNPLDSRS TEYATDVAKM
IQAPILHVNG DDPEAVLFVT QLAIDYRMQF KRDVVIDLVC YRRRGHNEAD EPSGTQPIMY
QQITKQRTTR ELYADRLTQG GVLDAERVQA KVDEYRNALD NGLHVVKSLV KEPNKELFVD
WRPYLGHAWT ARHDTRFDLK TLQELSAKLL EIPEGFVVQR QVSKIYEDRQ KMQAGGLPIN
WGYAETMAYA TLAFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDAGTYVPL QNLYKGQPRF
DLYDSFLSEE AVLAFEYGYS TTTPEALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVAVPT TPAQIYHLLR RQVIRPLRKP
LIVLTPKSLL RHKLAISTLE DLAEGSFQTV IPEIDALDPK KVERVVLCSG KVYYDLLEKR
RAEGRDDIAI VRIEQLYPFP EDDLNEVLAP YTNLKHIVWC QEEPMNQGAW YCSQHHMRRI
VGNHDKSLVL EYAGRDASAA PACGYASMHA EQQEQLLQDA FTV
//
