ID A0A238IY76_9RHOB Unreviewed; 987 AA.
AC A0A238IY76;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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:SMX22815.1};
GN ORFNames=BOA8489_00913 {ECO:0000313|EMBL:SMX22815.1};
OS Boseongicola aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Boseongicola.
OX NCBI_TaxID=1470561 {ECO:0000313|EMBL:SMX22815.1, ECO:0000313|Proteomes:UP000201838};
RN [1] {ECO:0000313|EMBL:SMX22815.1, ECO:0000313|Proteomes:UP000201838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8489 {ECO:0000313|EMBL:SMX22815.1,
RC ECO:0000313|Proteomes:UP000201838};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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}.
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DR EMBL; FXXQ01000002; SMX22815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238IY76; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000201838; 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:SMX22815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000201838};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 632..825
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 987 AA; 110095 MW; 6DC6FA7B2CB260DE CRC64;
MTEQSPNDIF KASSFLQGHN AEYIEQLYAR YAEDPDAVDE AWGAFFKELG DAGVDAQAEA
AGPSWARSDW PPQPSDELTA ALDGQWGDLG PQAAAAAGAK IAAKATEKGV PVSEDQIKRA
VLDSIRALMI IRAYRIRGHL VADLDPLGMR DQTPHPELDP KSYGFSESDM DRPIFIDNVL
GLQMASMREI IAIVNRTYCG TFALQYMHIS NPEEAAWLKE RIEGYGKEIA FTREGRKAIL
NKLVEAEGFE KFLHVKYMGT KRFGLDGGES LIPAMEQIIK RGGALGVKDI IIGMPHRGRL
SVLANVMAKP YKAIFNEFQG GSFKPEDVDG SGDVKYHLGA SSDREFDGNS VHLSLTANPS
HLEAVNPVVI GKARAKQDQH NDETRTSVLP LLLHGDAAFA GQGVVAECFG LSGLKGHKTG
GTIHIVVNNQ IGFTTAPHNS RSSPYPTDIA LMVEAPIFHV NGDDPEAVVH AAKVATEFRQ
KFGKDVVLDI FCYRRFGHNE GDEPMFTNPI MYQKIKKQKT TLSLYTERLV RDGLIPEGEI
EDMKAGFQAY LNEEFEAGKA YKPNKADWLD GRWSHLDKIG EKYQRGKTAI KQATFDEIGK
ALTTAPKGLP IHRTVERLFE NKAKMFETGE GFDWATAEAL AFGSLLTEGY PVRLAGQDST
RGTFSQRHSG IINQETEERY YPLNHIREGQ AHYEVIDSML SEYAVLGFEY GYSLAEPNAL
VLWEAQFGDF ANGAQIMFDQ FISSGERKWL RMSGLVMLLP HGFEGQGPEH SSARLERFLQ
MCAEDNWIVA NCTTPANYFH LLRRQLHRSY RKPLVIMTPK SLLRHKMAVS KTSEFITGSS
FHRVLWDDAQ HGNSDTELAA DDKIKRVVMC SGKVYFDLLE ERDARGIDDV YLMRVEQFYP
FPAQSFVNEL KRFPNADYIW CQEEPKNQGA WTFMEPNIEW VLTRIKAKNK RPKYVGRAAA
ASPATGLASA HKSQQQALVN DALTLEG
//
