ID M5E2Y3_9GAMM Unreviewed; 945 AA.
AC M5E2Y3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=TOL_1494 {ECO:0000313|EMBL:CCU71919.1};
OS Thalassolituus oleivorans MIL-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Thalassolituus.
OX NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU71919.1, ECO:0000313|Proteomes:UP000011866};
RN [1] {ECO:0000313|EMBL:CCU71919.1, ECO:0000313|Proteomes:UP000011866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIL-1 {ECO:0000313|EMBL:CCU71919.1,
RC ECO:0000313|Proteomes:UP000011866};
RX PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA Yakimov M.M., Teeling H., Golyshina O.V.;
RT "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL Genome Announc. 1:1-3(2013).
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; HF680312; CCU71919.1; -; Genomic_DNA.
DR AlphaFoldDB; M5E2Y3; -.
DR STRING; 187493.CN03_10700; -.
DR KEGG; tol:TOL_1494; -.
DR PATRIC; fig|1298593.3.peg.1430; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR Proteomes; UP000011866; Chromosome.
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:UP000011866};
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 945 AA; 107041 MW; 5D16429187C1BAB6 CRC64;
MHEHTMEQLW STSQLSGGNV AYIEELFETY LRDPNEVPEE WRNYFDQLPR VDESTSVDTP
HKPIREQFLL LSKNQHRSRP ASQGSVSSDF ERKQVQVLQL INAYRGRGHQ HAKLDPLGLM
VRESVPDLDL QFHGLSRADL DTVYQTGSLF IGQAEAPLKD IVDALERTYC STVGSEYMHI
VNTVEQRWFQ QRLESVRAHP KYGEEVKLHL LERLTAAEGL EKYLGSRYPG VKRFGLEGGE
SLIPLMDELI QRSGTYGAKE IVIGMAHRGR LNTLINTLGK KTSDLFDEFD GKASYQSHGD
VKYHQGFSSN VMTSGGEVHL ALAFNPSHLE IVSPVVEGSV RARQDRRKDK TGEKVVPVLI
HGDAAFAGQG VVMETFQLSQ TRAYKTGGTI HIVINNQVGF TTSKREDVRS TEYCTDVAKI
VEAPILHVNG DDPEAVLFVT QLAVDYRNEF KKDVVIDLVC YRRRGHNEAD EPSGTQPLMY
AKIKAQPTTR TLYAERLIAE STLTEEYSKQ LEEEYRTALD NGQHVVKSLV KEPNTELFVD
WTPYLGHEWT TKADTTFDVK RLQELAHQMQ EIPDGFQVQR QVEKIMEDRR RMAAGAMPIN
WGFAEVMAYA TLVDQGHAVR ITGQDVGRGT FSHRHAILHN QKDGVAYSPI ANLSADQAPF
ELYDSLLSEE AVLGFEYGYA TTTPGTLVIW EAQFGDFANG AQVVFDQFIS SGEHKWGRLC
GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNVQICVPS TPAQVYHMIR RQAIRPLRKP
LVVMSPKSLL RHKLATSTLE ELTDGRFRTC LDEIDQIEPE KVDRILMCSG KVYYDLLERR
RAEEIDNIAI VRIEQIYPFP AKQLTKLLSK FTNASEIYWV QEEPMNMGAW FSSQHHMRRV
AEDLNPKLHL KYAGRDLSAS PAAGYMALHL KQQEQLIRDA LNLAG
//
