ID A0A3N5BK96_9BACI Unreviewed; 943 AA.
AC A0A3N5BK96;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=EDC24_2926 {ECO:0000313|EMBL:RPF50108.1};
OS Aquisalibacillus elongatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aquisalibacillus.
OX NCBI_TaxID=485577 {ECO:0000313|EMBL:RPF50108.1, ECO:0000313|Proteomes:UP000276443};
RN [1] {ECO:0000313|EMBL:RPF50108.1, ECO:0000313|Proteomes:UP000276443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18090 {ECO:0000313|EMBL:RPF50108.1,
RC ECO:0000313|Proteomes:UP000276443};
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 (NOV-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:RPF50108.1}.
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DR EMBL; RKRF01000014; RPF50108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5BK96; -.
DR Proteomes; UP000276443; 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; IPR032106; 2-oxogl_dehyd_N.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000276443};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 596..792
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT COILED 494..532
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 943 AA; 106683 MW; EBFF29CF305D63C5 CRC64;
MAIKGSNDNV WDAFHGPNMG YIEEQYDLYL DDPDAVDESL RQMFDEHGAP SWVSESTLDT
SSAQQGASTA DLQKLTATMK LVEAIRRHGH LEADIFPVGK QDDRYSPLVD PKKYGLSEGD
LKQLDAKLLT SEVPRNVKNA WDLVQHLKKR YSGTISYEFN HIPDDDEREW LYQKVETGAF
DVSLNNEEKK EVLKRLGDVE GFEQFLAKQF VAQKRFSIEG LDVMVPMLDR MVMNAHNDDV
DHVLMGMAHR GRLNVLAHVL GKPYDMIFSE FAHAPDKTLV PSEGSTGINY GWTGDVKYHF
GADREFIDDD ESKTKITLAH NPSHLEFVNP VVTGYTRAVQ DNRDEKGYAK NDPSKAFNIQ
IHGDAAFIGE GVVAETLNLS QLRGYETGGS IHVIANNLVG FTTDHEDGRS TKYASDLAKG
FEIPVIHVNA DDPVACLTAV ELAYQYRTTF EKDVLIDLVG YRRYGHNEMD EPRGTQPELY
QDIDNQPTAY EVYADRLVKE NILTEEEAKS YKEDVKKKLR EIFDNMTESE KKNPSVPDLP
EEVVNGLDKI ETAVDVDTLK KLNEDMLKRP DGFEVFRKLE KILKRREKAF NEGEKIDWAL
GEALAFASIL NDGTPIRMSG QDSERGTFAH RHAVLNDVNS KQKYSPFHGL EGVNKSFSIY
NSPLSEAGVL GFEYGYSVQS DDTLVLWEAQ YGDFANAAQV IFDQFIAAGR AKWGQIASMV
MLLPHGYEGQ GPEHSSARLE RFLQLSAENN WTVANVTTSG QYFHLLRRQA AIVGTEAARP
LVLMTPKSLI RNQHVAVEPE KLVEGKFQTV LEQEGLGENP DSVKRLVIGS GKVMVDIEEH
MEDQDPNDEL HVIRLEQIYP FPEKELKNIL KKYKNVEEII WIQEEPKNMG SWDFVKERIQ
SIKKVKQKLE YVGRPYRSSP AVGDPNIHKS EQNRIINEAL TLD
//
