ID C5BL86_TERTT Unreviewed; 945 AA.
AC C5BL86;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:ACR10789.1};
GN OrderedLocusNames=TERTU_2522 {ECO:0000313|EMBL:ACR10789.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR10789.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR10789.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001614; ACR10789.1; -; Genomic_DNA.
DR RefSeq; WP_015816901.1; NC_012997.1.
DR AlphaFoldDB; C5BL86; -.
DR STRING; 377629.TERTU_2522; -.
DR KEGG; ttu:TERTU_2522; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000009080; 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:ACR10789.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 600..793
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 945 AA; 106615 MW; 0040BDE46AD442E3 CRC64;
MQDSLMELLW KTSHISGGNA AYVEEVYEEY LQDPGSVPEQ WRDYFDQLPK VNGGTGVDVR
HSEIVEYFEL LGRNRARPMV APGSGAADIA HERKQVEVVQ LVNAYRLSGH QKADLDPLRL
RERKSPQDLD LSFHNLNVAD LDSVFQTGDL SFGYKEGTLN QIIGDLEQTY CGKIGSEVMH
ITNYEERRWL LQRLESSRAR PDLGPKAKQY LLKRLTAAEG LERHLDSKYP GTKRFGLEGG
ESLIPTLDTL IKRCGTYGAK EMVIGMAHRG RLNTLVNVLG KNPSDLFDEF EGKKLVDTSG
DVKYHQGFSS NVMTPGGEMH LALAFNPSHL EIVSPVVQGS VRARQDRRDD QRGNMVVPVV
IHGDAAFAGQ GVVMETFQMS QTRAYRTGGT VHLVINNQVG FTTSRQDDSR STTYATDVAK
MIEAPIFHVN ADDPEAVVFV TNLAADYRNE FRKDVVIDLV CYRRRGHNET DEPSATQPLM
YKAIRSHKTT RTLYAEQLVN DGVITQDEAE GYLNDYRAKL DRGEDVAEGL VSEPDSSLFV
NWSPYIGHDW QTPYESGYPI KDLQALAEQI SSIPDGVQVQ RQVAKIYDDR RKMAGGALPI
NWGMAETLAY ATLLKQGYRV RITGQDVGRG TFSHRHAVVH NQKDGSCYLP LEHVDENQGP
LDIYDSYLSE EAVLAFEYGY ATTTPGGLTI WEAQFGDFAN GAQVVIDQFI TSGEHKWQRL
CGLTMLLPHG YEGQGPEHSS ARLERFMQLC AEHNIQVCIP TTPAQVYHML RRQAIRYMRR
PLVVMSPKWI LRHKLATSTL EELADGRFET VIGDCEAEAS EVKRVILCSG KVYYHLYEAR
EEREQKDVAL IRIEQLYPFP EEDLRMTLKP YAHVTDVIWC QEEPMNQGAW FSSHHRMRRV
VERVNEDAYL RYVGRASSSA PAAGYMSTHL DELNKFINAA LDTSV
//
