ID F5XX26_RAMTT Unreviewed; 956 AA.
AC F5XX26;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
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:AEG92970.1};
GN OrderedLocusNames=Rta_18790 {ECO:0000313|EMBL:AEG92970.1};
OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS TTB310).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG92970.1, ECO:0000313|Proteomes:UP000008385};
RN [1] {ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA Barras F., Heulin T.;
RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG92970.1, ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RX PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA Vermeglio A., Achouak W., Heulin T.;
RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL PLoS ONE 6:E23784-E23784(2011).
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 -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
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DR EMBL; CP000245; AEG92970.1; -; Genomic_DNA.
DR RefSeq; WP_013901202.1; NC_015677.1.
DR AlphaFoldDB; F5XX26; -.
DR STRING; 365046.Rta_18790; -.
DR KEGG; rta:Rta_18790; -.
DR PATRIC; fig|365046.3.peg.1915; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_4; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000008385; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008385};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 603..800
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 956 AA; 106499 MW; 4AC2D295849D6568 CRC64;
MSETNSVYTA YQANSYLFGG NAPYVEEMYE NYLTNPGSVP DNWREYFDAL QHVPAVDGSN
AKDVPHLPVV NAFAERAKQG GTKVVVASGA DSEMGRKRTA VQQLIAAYRN VGARWADLDP
LKRTEREKIP ELDPAFYGFT DADQETVFNT SNTFFGRDTM SLRELINALR ETYCGTIGAE
YMYITDQGRK RWWQQKLESI RSKPQFNADR KKHLLDRLTA AEGLERFLHT KYVGQKRFSL
EGGESFIAAM DELIQQAGAK GVQEIVIGMA HRGRLNVLVN TLGKMPRDLF AEFEHTAKED
LPAGDVKYHQ GFSSDVTTPG GPVHLSLAFN PSHLEIVNPV VEGSVRARMD RRGDPKGRQV
LPVQVHGDAA VAGQGVVMET LALAETRGYF TGGTVHLVIN NQIGFTTSDP RDSRSTLYCT
DVVKMIEAPV LHVNGDDPEA VVLATQLALE YRQEFAKDVV VDIVCFRKLG HNEQDTPSLT
QPLMYKKIAA HPGTRKLYAD KLATQGLGDS LGDDMVKAYR AAMDAGRHTV DPVLTNFKSK
YAVDWSPYLG KKWTDAAETA IPTAEWKRLA ERITTVPENF TVHPLVKKVL EDRAAMGRGD
VNVDWGMGEH MAYASLVASG YPVRLSGEDV GRGTFTHRHA VLHDQNRERW DVGTYIPLQN
VADSQAPFVC IDSILSEEAV LGFEYGYASN DPNTLVIWEA QFGDFANGAQ VVIDQFIASG
EVKWGRVNGI TLMLPHGYEG QGPEHSSARL ERFMQLSADT NMQVVQPTTA SQIFHVLRRQ
MIRPLRKPLV IMTPKSLLRN KDATSPLSEF TKGGFQTVIP ENQELKADKV KRVIVCSGKV
YYDLAKKREE KGADDTAILR VEQLYPFPHK VFASELRKYP NATDIVWCQD EPQNQGAWFF
VQHYIHENML EGQKLGYAGR AASASPAVGY SHLHQEQQKA LVDAAFSKLK GFVLTK
//