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Database: UniProt
Entry: Q98ED0_RHILO
LinkDB: Q98ED0_RHILO
Original site: Q98ED0_RHILO 
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
//
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