ID A0A069DES8_9BACL Unreviewed; 970 AA.
AC A0A069DES8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=TCA2_0620 {ECO:0000313|EMBL:GAK38894.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK38894.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK38894.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK38894.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
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:GAK38894.1}.
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DR EMBL; BBIW01000001; GAK38894.1; -; Genomic_DNA.
DR RefSeq; WP_047910052.1; NZ_BBIW01000001.1.
DR AlphaFoldDB; A0A069DES8; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000028160; 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:UP000028160};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 612..808
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 970 AA; 108566 MW; C94264279FA786C8 CRC64;
MANEDGNMQS PWKTYYGPNF GYVQEQFEIY SADPEAVDAE FRTLFKDWGP PPMDVGTDHN
HGLASSGTGS SASSGVVDLQ LLQKAVTAGK LVQNIRRFGH LVADIDPLQL DVKTEESLLT
PSKLGLSEQD LRAIPASIIW ENADSQTMTG LDAIQRLRDI YTGPLAYEFN HIQDEEERNW
LYQSIESGAQ AAQLTSDERK SLLARLVEVE QFEQFLHKNF VGQKWFSIEG NDVLVPMLDK
IIEIMAEAGS SHILMGMAHR GRLNVLAHVL GKPYGKIFSK FHQANNKDLV PSESSSGVNY
GWTGDVKYHL GATRYVKKGE VVQAKITMAN NPSHLEYVNP VVQGFARAAQ DDRGQAGYPK
QDVTKAATII MHGDAAFPGE GIVAESLNLK SLKGYQNGGT IHIIVNNRIG FTTNSDASRS
TMYSSDLAKG YEIPIIHVNA DNPDACMAAI RLASEYRNKF NKDFLIDLIG YRRYGHNETD
DPETTQPLVY SKVKNHPTVC ELYAEVLVQS GAGEKELLTN LRNAAQNQLK QAYDEVKQGT
VSHEEVHDKV DAGSTELQRP ERLTNAQTAV PIEKLREINA ELLKWPEGFK VYPKLQRILQ
RRQNALNEGE KVDWSLAETL AFATILADGK PIRMSGQDSQ RATFAHRNLV LHDSETGDSY
NVLHRLPQAK ASFALYNSPL SEESVVGFEY GYNVYAPETL VIWEAQFGDF ANCAQVLFDQ
FVSSGRSKWS QNSSLVMLLP HASEGQGPEH TSARLERFLQ MCADDNWIVA NLSSSAQYFH
LLRRQAALTE TDDARPLVLM SPKSLIRNPR VASPAKEFSE GSFHSVLEEP ILGAAPDKVE
RILLCSGKIA IDLEEAIDKE KGEDWSWLHI LRVEQLYPFP EQEIRRFLAR FRNVKEIVWT
QEEPKNMGAW TYMEPRLRDL LPAGVKLDYA GRPERSSPAT GFQHVHVVEQ QQILSKVLKQ
SSKKNIPLGR
//
