ID A0A231R7L1_9BACL Unreviewed; 964 AA.
AC A0A231R7L1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B1A99_23570 {ECO:0000313|EMBL:OXS55257.1};
OS Cohnella sp. CIP 111063.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1955714 {ECO:0000313|EMBL:OXS55257.1, ECO:0000313|Proteomes:UP000215193};
RN [1] {ECO:0000313|EMBL:OXS55257.1, ECO:0000313|Proteomes:UP000215193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 111063 {ECO:0000313|EMBL:OXS55257.1,
RC ECO:0000313|Proteomes:UP000215193};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Cohnella sp SGD-V74 (T) CIP 111063, whole genome shotgun sequencing
RT project.";
RL Submitted (MAR-2017) 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:OXS55257.1}.
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DR EMBL; MWSG01000017; OXS55257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231R7L1; -.
DR Proteomes; UP000215193; 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:UP000215193};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 603..799
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 532..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 106885 MW; F50A3A4AE0F04B18 CRC64;
MSVDNEKMQE LWQQFFGPNL GYVQEQYDIY LQDAEAVSPQ YRELFAQYGA PPRVDAASAY
PASAPQGSGG SASLDANLLK KAIAAGQLAW NIRSFGHLAA DIDPLELSPK ANTEMIEPAT
YGLTEADLRQ LPPDCVWEDA PYPLSNAWEA VQKLLQVYTG PIAFEFGHVH VEEERKWLNK
QAETVIPSTK LLASEKESLL RKLYEAEQFE DFLQRTFVGQ KRFSAEGIEA LVPLTDEIVH
ELTNDGARHI AMGMAHRGRL NVLAHVLGKP YGNVFAEFHH SPNKNLIPSE GSIGINYGWT
GDVKYHLGAN RSISSGETAE TRITLANNPS HLEYVNPVVG GFARAAQEDR SQPGYPVQNL
DLAASILIHG DAAFIGEGIV AETLNFNNIK GYTCGGTIHI IANNRIGFTT ESHDSRSTHY
ASDLAKGFEI PIVHVNADDP EAVIAAARMA SEYRTLFKKD FVIDLIGYRR YGHNETDDPE
TTQPLIYKKV KAHPNVARLY ADKLVREGAL SEEAANQIKR DVQNKLKDAY DEVKGREGNS
PVRQSHPPEF SLDAPKPVTA VPLEKLRSIN AGLLKFPESF NVYGKLKRIL ERRADALNDG
EKVDWSHAET LAFATILADG TPIRLSGQDA ERATFAHRNL VLHDTETGDT FCPLHAIPEA
KASFAIHNSP LSEAGVLGLE YGYNVFAPET MVIWEAQFGD FANSAQVLID QFISAGQSKW
SQRSGLTMLL PHGYEGQGPE HSSARLERFL QLSGEENWTV AYLSSAAQYF HLLRRQASVL
NTDQARPLVL MAPKSMIRNP YVASSAAELS EGTFQTVLEQ PGLGGQPAKV ERIVLCTGKV
AIDLAEELAK TPDTNRDWLH IVRVEQLYPF PKLELKAILD RFPNLSEVLW VQEEPKNMGA
WGYIEPRIRE LVDVAKVSVS YNGRPKRSSP ASGYQQIHTF EQQFIINQTL VQKKKTKSAV
KSGR
//
