ID A0A1N6J9V1_9RHOB Unreviewed; 990 AA.
AC A0A1N6J9V1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=SAMN05444722_1971 {ECO:0000313|EMBL:SIO41158.1};
OS Rhodovulum sp. ES.010.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1882821 {ECO:0000313|EMBL:SIO41158.1, ECO:0000313|Proteomes:UP000184943};
RN [1] {ECO:0000313|EMBL:SIO41158.1, ECO:0000313|Proteomes:UP000184943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES.010 {ECO:0000313|EMBL:SIO41158.1,
RC ECO:0000313|Proteomes:UP000184943};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FSRS01000001; SIO41158.1; -; Genomic_DNA.
DR RefSeq; WP_074219926.1; NZ_FSRS01000001.1.
DR AlphaFoldDB; A0A1N6J9V1; -.
DR STRING; 1882821.SAMN05444722_1971; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000184943; 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 Reference proteome {ECO:0000313|Proteomes:UP000184943};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 634..827
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 990 AA; 111242 MW; 07D3BF5300943A85 CRC64;
MTDQSANETF HNSSFLQGHN AEYVEQLYAR YANDPDAVDE QWRRFFAELG DDEVSVKREA
AGPSWARRDW PPAPSDEITA ALDGQWPGLP VEKEAKATEE KIREKAQEKG VAVTDDEVKR
AVLDSIRALM LIRAYRIRGH LVADLDPLGM RNPTPHPELD PGSYGFTEAD MERPVFIDNV
LGLQVASMRE ILAIVKRTYC GTFALQYMHI SDPEQSAWLK ERIEGYGKEI KFTREGRRAI
LNRLVEAEGF EKFLHVKYMG TKRFGLDGGE ALIPAMEQII KRGGALGLEE IAIGMPHRGR
LSVLANVMGK PYKAIFHEFQ GGSFKPEDVD GSGDVKYHLG ASSDREFDGN VVHLSLTANP
SHLEAVNPVV LGKTRAKQSQ MRDYDRKKVV AVLLHGDAAF AGQGVVAEGF GMSGLVGHRT
GGTIHIVVNN QIGFTTAPHF SRSSPYPTDI ALMVEAPIFH VNGDDPEAVT HAAKVATEFR
QKFGKDVVID MFCYRRFGHN EGDEPMFTNP LMYNKIKKHK TTLQLYTDRL VADGLIPEGE
IEDMKAAFQS HLNDEFESAK EYKPNKADWL DGRWSHIERG GGDDYQRGDT AISEDTMQAL
GQALTTVPEG FALHRTVGRL LQAKKEMFDS GKGFDWATAE AMAFGSLLTE GYPVRLSGQD
STRGTFSQRH SALINQDSEE RYYPLNHIRK GQARYEVIDS MLSEYAVLGF EYGYSLAEPN
ALVMWEAQFG DFANGAQIMF DQFISSGERK WLRMSGLVVL LPHGYEGQGP EHSSARLERF
LQMSAEDNWI VANCSTPANY FHILRRQLHR SFRKPLILMT PKSLLRHRLA VSEAKAFLTG
SSFHRVLWDD AETHRSSDLT LKPDDQVRRV VLCSGKVYYD LLEERDARGI DDVYLMRIEQ
FYPFPALSLV KELERFKEAE MIWCQEEPKN QGAWTFIEPN LEWVLGRIDA KHNRPRYVGR
PAAASPATGL ASQHKAQQAA LVDDALTIEG
//
