ID Q98ED0_RHILO Unreviewed; 995 AA.
AC Q98ED0;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 24-JAN-2024, entry version 108.
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 OrderedLocusNames=mll4301 {ECO:0000313|EMBL:BAB50990.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB50990.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB50990.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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 -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
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DR EMBL; BA000012; BAB50990.1; -; Genomic_DNA.
DR RefSeq; WP_010912332.1; NC_002678.2.
DR AlphaFoldDB; Q98ED0; -.
DR KEGG; mlo:mll4301; -.
DR PATRIC; fig|266835.9.peg.3394; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OMA; RDSYCRT; -.
DR Proteomes; UP000000552; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 641..834
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 995 AA; 111873 MW; 22BD09264FD6C8D7 CRC64;
MARQDQTNDQ FSLTSFLYGG NADYIDALYA AYEDDPASVN PEWQEFFAGL KDDAGDVRRN
AKGASWAKPS WPLQANGELV SALDGNWGIV EKHLEKKVKD KAVTNGVVLS DADVHQATRD
SVRAIMMIRA YRMRGHLHAN LDPLGIAKPL EDYNELSPEN YGFTAADYDR PIFLDNVLGL
EFGTIRQMLE ILTRTYCSTL GVEFMHISDP EEKAWIQARI EGADKEISFT NTGKKAILQK
LVEAEGFEQF IDVKYKGTKR FGLDGGEALI PALEQIVKRG GQLGMKEIVL GMAHRGRLNV
LSQVMAKPHR AIFHEFKGGS AAPDEVEGSG DVKYHLGASS DREFDGNKVH LSLTANPSHL
EIVDPVVMGK ARAKQDYLFG RGREEIVPLE ERAKVLPLLL HGDAAFAGQG VIAEILGLSG
LRGHRVAGTL HFIINNQIGF TTNPRFSRSS PYPSDVAKMI EAPIFHVNGD DPEAVVHATK
VAIEFRMKFH KPVVVDMFCY RRFGHNEGDE PAFTQPIMYR NIRTHKTTVQ IYADRLIAEG
HITQAELDQM KADWRAHLES EWEVGQHYKP NKADWLDGAW SGLRTADNQD EQRRGKTAVP
VKTLKEIGKK LTEVPKGFEA HKTIIRFLEN RREAIESGEG IDWSTAEALA FGAILLDGNP
IRLSGQDSER GTFSQRHSVL YDQRDETRYI PLNNLSAAQA GYEVINSMLS EEAVLGFEYG
YSLAEPKALT LWEAQFGDFA NGAQVVFDQF ISSGERKWLR MSGLVCLLPH GYEGQGPEHS
SARLERFLQL CAEDNMQVAN CTTPANYFHI LRRQLKRDFR KPLILMTPKS LLRHKRAVST
LPEISGESSF HRLLWDDAQL LPNQPIKLTK DSKIRRVVLC SGKVYYDLYE EREKRGINDI
YLLRVEQLYP FPAKALITEL SRFRNAEMVW CQEEPKNMGA WSFIDPYLEW VLAHIDAKHQ
RVRYTGRPAA ASPATGLMSK HLAQLAALLE DALGE
//