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Database: UniProt
Entry: F5XX26_RAMTT
LinkDB: F5XX26_RAMTT
Original site: F5XX26_RAMTT 
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
//
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