ID U5N595_9BURK Unreviewed; 985 AA.
AC U5N595;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:AGX86425.1};
GN ORFNames=Cenrod_0301 {ECO:0000313|EMBL:AGX86425.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX86425.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX86425.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX86425.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(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};
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; CP004885; AGX86425.1; -; Genomic_DNA.
DR AlphaFoldDB; U5N595; -.
DR STRING; 946483.Cenrod_0301; -.
DR KEGG; cbx:Cenrod_0301; -.
DR PATRIC; fig|946483.4.peg.300; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_4; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000017184; 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:UP000017184};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 620..817
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 985 AA; 108967 MW; F09A242B5EB6D93E CRC64;
MDETLPENPS QSLYQVLRAY SHLFAGSASY IEDAYERYLD DPDSVAASWR EWFDTLAAAP
ASDGGKAPDV PMRAAVEAFA ARVRYERAGE WSPGWSSASA ACPLDSTPGR KHTAAQQLIA
AHRNIGVRWA SLDPLQRAGR PDIPELDPSF YGLEDADLDL EVDTSNTFFG PATMSVHALL
DALRTTYCGV LGAEFMYLTD QRQKRWWQHK LESIQSQPAI NADGKRHILE RLTAAEGLER
FLHTKYVGQK RFSLEGGESF IVAMDELIQR AGARGVEEIC IGMAHRGRLN VLVNTLGKLP
KDLFAEFDHT APEELAAGDV KYHQGFSSDI ETPGGPVHLS LAFNPSHLEV VNPVVEGAAR
ARMDRRGDPT GKKVLALLVH GDAAFAGQGV NQETLALAQT RGYTTGGTVH LIINNQIGFT
TSDPRDLRST VYCTDIVKAV EAPVMHVNGD HPESVVLAVQ WALDYRMEFG KDVVVDIVCY
RKLGHNEQDT PALTQPLMYK KIAQHPGVRQ LYAERLAVEG LGNTLGDDMA RAYRAAMDTG
KRTAVSVLGV HKYPFAIDWT PYLAGRSDDE GMDCRTAIPL ERWASLAQRL TTLPPTLTLH
PLVRKVYEDR AAMGRGDIPV DWGMGEHMAF ASLVAQGVPV RLSGEDSGRG TFSHRHAVIH
DQNREKWDEG TYVPLQNVAE GQAPFVVIDS ILSEEAVLGF EYGYASNAPD ILVAWEAQFG
DFVNVAQVVI DQFLASAQVK WGRLNGLTLL LPHGQEGQGP EHSSARIERF MQLAADDNMQ
LVQPTTASQI FHVLRRQMLR KVRKPLVVFT PKSLLRHRDA ASPIAEFTDS VFRTVIDDAQ
ATEPDTVQRV LLCSGKVYYD LVKKRAALEA RHVAIVRIEQ LYPFPHAALL RVWERYPVAT
EWLWVQDEPR NQGAWFFVQH CLAEHLLARQ RLGYCGRAPS SSPAVGYAHL HQEQQRALVD
GAFAPDPAGL GASFCGWRTH AQPVA
//
