ID A0A0F2RQV6_9RHOB Unreviewed; 986 AA.
AC A0A0F2RQV6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN Name=sucA {ECO:0000313|EMBL:KJS40350.1};
GN ORFNames=VR71_23420 {ECO:0000313|EMBL:KJS40350.1};
OS Roseovarius sp. BRH_c41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS40350.1, ECO:0000313|Proteomes:UP000033676};
RN [1] {ECO:0000313|EMBL:KJS40350.1, ECO:0000313|Proteomes:UP000033676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS40350.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJS40350.1}.
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DR EMBL; LADY01000069; KJS40350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RQV6; -.
DR PATRIC; fig|1629709.5.peg.452; -.
DR Proteomes; UP000033676; Unassembled WGS sequence.
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:KJS40350.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 630..823
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 986 AA; 110520 MW; 68AF0B110977EEF8 CRC64;
MTDQSPNDLF HASSFMQGHN AEYLEQLYAR YANDPNAVDA AWTNFFDALG DGDDDVKAEA
AGPSWARADW PPMPADDLTA ALTGEWPAEP ELKDAGKKIT AKAAEKGVSV SDEDVKRAVL
DSVRALMLIR AYRIRGHLAA DLDPLGLRET PLRPELDPKS YGFTEIDMDR PIFIDNVLGL
QIASLREILA IVRRTYCGTF ALQYMHISDP EESAWLKERI EGYDKEITFT RTGRKAILNK
LVEAEGFEKY LHVKYMGTKR FGLDGGESLI PAMEQIIKRG GQLGVEDIVI GMPHRGRLSV
LANVMGKPYR AIFNEFQGGS FKPEEVDGSG DVKYHLGASS DREFDGNRVH LSLTANPSHL
EAVNPVVIGK VRAKQDQLND TDRTKVLPIL LHGDAAFAGQ GVVAECFGLS GLKGHRTGGT
IHLVVNNQIG FTTAPHFSRS SPYPTDIALM VEAPIFHVNG DDPEACVHAA RVATEFRQKF
HKDVVIDMIC YRRFGHNEGD EPMFTNPVMY KKIKQQKTTL SLYTERLVKD GLIPEGEIED
MKTAFQAYLA DEFDAGKDYR PNKADWLDGK WADLNAHRGK YERGETAIKP ETMAQVGRAL
STAPEGFPLH KTVERLLESK ANMFETGTGF DWATAEALAF GSLLTEGYRV RLSGQDCTRG
TFSQRHSGLI NQDNEDRYYP LNHIRDGQAH YEVIDSMLSE YAVLGFEYGY SLAEPNALTL
WEAQFGDFAN GAQIMFDQFI SSGESKWLRM SGLVCLLPHG YEGQGPEHSS ARLERFLTMC
GGDNWIVANC TTPANYFHIL RRQMYRTFRK PLILMTPKSL LRHKMAVSKT EEFITGSSFH
RVLWDDAQYG NSETKLVGDK KIKRVVMCSG KVYYDLLEER DNRGIDDVYL MRIEQFYPFP
AMSLVKELER FKGAEMVWCQ EEPKNQGAWS FIEPNIEWVL TRIKAKHLRP VYAGRPASAS
PATGLAKQHK AQQEALVDAA LTIEGK
//
