ID A0LP65_SYNFM Unreviewed; 901 AA.
AC A0LP65;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Sfum_3547 {ECO:0000313|EMBL:ABK19217.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK19217.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK19217.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP000478; ABK19217.1; -; Genomic_DNA.
DR RefSeq; WP_011700342.1; NC_008554.1.
DR AlphaFoldDB; A0LP65; -.
DR STRING; 335543.Sfum_3547; -.
DR KEGG; sfu:Sfum_3547; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_7; -.
DR InParanoid; A0LP65; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001784; 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 ECO:0000313|EMBL:ABK19217.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 564..757
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 901 AA; 101344 MW; 7A083F8661CED227 CRC64;
MEFSIGWNAD YIDAQYRLWK SDPKKVSREW RIFFEGFELA SFPEPSGICD REEVLLQAGV
QELIHRYRDI GHLLACLDPL ASCPIDHPLL RLSSFNLSEA ALDRNVQAPG FLHSKRMPLR
EIVSILRDTY CGSVGVEYMH LQDPSERAWL QDRMEPIRNR PDPAADEKLA ILSVLTRATL
FEQFLHTKYV GQKRFSLEGA EVVTAMLDSL LRRAAEAQCR EVILGMAHRG RLNVLVNVLR
KPYSDIFCEF EDHYDPESMV GSGDVKYHKG YMADLEIPGG RSLRVLLAAN PSHLEAVDPV
VEGIARARQD GCGDCLRRQV LSVLLHGDAA FAGQGVVAET LNLSLLEGYS TGGTIHVVVN
NQIGFTTLPD HARSTRYSTD VAKMLMVPIF HVHGEDPEAA CFLVKLALDY RMEFAKDVVI
DVVCFRRYGH NEGDEPYFTQ PVMYDRIKER PQLWRGYAAK LRDEGVVSDG EIEAMQDGIR
ECLEKAFDSV HDKTCPLPVN RFIESWDDIG RDDPETPVET GVAEETLVSL ARGMNAFPSG
FSVHPRLERI LARRLESVEK GEGIDWATAE LLAFGTLLEE RTPVRLSGQD SLRGTFSHRH
SVLTDVKTGE RFTPLNALSP RQARYCGYDS MLSENAVLGF EYGYSLAEPR TLVIWEAQFG
DFANNAQVMI DQFISSGETK WQRRSGLVLL LPHGLEGQGA EHSSARLERF LQLCAEDNIQ
VCNPSTPAQY FHLLRRQVKR NVRKPLVVMA PKSLLRHPLA VSAMADLSVG RFREVLDDPG
ESEAPERVLF CSGKIYYDLV GKRDEARTGR IPIIRIEQFH PFPERLLEEI AAKRSRAGEW
VWVQEEPRNM GGWGFVGPRL EALTGREVGF IGRKAAASPA TGSHRAHLAE QEAILREALK
L
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