ID A0A366EA78_9BACI Unreviewed; 950 AA.
AC A0A366EA78;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {ECO:0000256|HAMAP-Rule:MF_01169};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01169};
GN Name=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN ORFNames=DES48_105169 {ECO:0000313|EMBL:RBO98318.1};
OS Paraliobacillus ryukyuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX NCBI_TaxID=200904 {ECO:0000313|EMBL:RBO98318.1, ECO:0000313|Proteomes:UP000252254};
RN [1] {ECO:0000313|EMBL:RBO98318.1, ECO:0000313|Proteomes:UP000252254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15140 {ECO:0000313|EMBL:RBO98318.1,
RC ECO:0000313|Proteomes:UP000252254};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) 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|HAMAP-Rule:MF_01169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|HAMAP-Rule:MF_01169};
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|HAMAP-
CC Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_01169}.
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:RBO98318.1}.
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DR EMBL; QNRI01000005; RBO98318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366EA78; -.
DR STRING; 200904.GCA_900168775_01134; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000252254; Unassembled WGS sequence.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01169; SucA_OdhA; 1.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
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; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01169};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01169}; Reference proteome {ECO:0000313|Proteomes:UP000252254};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 593..789
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 950 AA; 108859 MW; 6080063D36A4A269 CRC64;
MTQKESNKRF WRNIHQANRS YMEEQYLLFL QDPKQVPSSI QEIFNTYGAP NWPGIANYKS
QRNESDHTNS TKKIKATIQL ADAIRRFGHL SATIYPVGTK KHRHNELIDL KTYDLTIEDL
KQLPAQIIWG NPSSSMTNAW DVIQALTQTY AKTIAFEYDH VNQNKERKWL EKQIESNTYQ
VTFSNEQKQQ LLKALIDVEG FEHFLAKTFV AQKRFSIEGL DSMVPMLDYL VQQSLYDDTE
NVLIGMAHRG RLSVLTHILG KPFDILFSEF YHAQDKTLVP SSTSSITYGW TGDVKYHFGA
KRQFGEGKPA PTKVTLAHNP SHLEFVNPVV QGFTRAHQDF RFESGYPTQK WQRACSIMIH
GDAAFMGQGV VAETLNLSAI EGYQTGGTIH LIANNQIGFT TNYRQSRSTR YASDLAKGFE
IPIIHVNADD PEACLSAMKL AYQYRKKFHK DFLIDLIGYR RYGHNEMDEP RATQPLAYQE
IDQHPTVVDI YRGQLEAAKV ITSTDCENWR QEVHTKLQEI YLNMKENQFE EWIQSEPGAL
KNELTNIQTN VTYDKLRRFN HDLLKRPARF VGFNKLERLL QKRAKVFDEQ QIVDWAMAEI
LAFATVLSDG IPIRLTGQDT ERGTFAHRHL VLHDINSDET YCPLHGISEA KASFAIHNTP
LSEVAVLGFE YGYSVEAPKT LVMWEAQFGD FANVGQVIFD QFISAGRAKW GEKSNMIVLL
PHGYEGQGPD HSSARMERFL LTAAENNWII ANVTTSANYF HLLRRQASLV NSDAARPLII
MTPKSLLRHK QVVSNVDALV HDNFQPIIAK QKQTNQPVTR LIIGSGKIMV EFDELNDCQS
FNWLTTIRLE QIYPFPKTLL QELLLDYPDV TEVIWLQEEP RNMGAWHFVK EKIACVLHEN
VVLLYVGRGD RSSPAVGNMK VHLKEQKYIL ETAMKDVTSI ITTEYGFCKE
//
