ID A0A268E4T0_9BACI Unreviewed; 944 AA.
AC A0A268E4T0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=sucA {ECO:0000313|EMBL:PAD68128.1};
GN Synonyms=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN ORFNames=CHH83_15135 {ECO:0000313|EMBL:PAD68128.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD68128.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD68128.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD68128.1,
RC ECO:0000313|Proteomes:UP000216230};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-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:PAD68128.1}.
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DR EMBL; NPCL01000062; PAD68128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268E4T0; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000216230; 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 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:UP000216230};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 594..790
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 944 AA; 107032 MW; 858DEB11BF56915A CRC64;
MSEGTLKKKF PWEDFHGPNL GYVMEQYDRY KTDPNSIDIE LKEIFDNWGS PSIQTNEVTF
ATEETISADK MKKVAEAVNL ATNIRRYGHL NAAIYPLEEN KTKNEFLLLE SYDLTKEDLK
EIPAHLICED APDHVSNGLE AFQYLKEVYK KSIAFEFSHV HNYEEKTWLV KQVESGVIFK
DLSNEKRKSI LKRLTEVEGF EQYLHRTFVG QKRFSIEGLD MLVPILDELI SSAVEVGTNT
INIGMAHRGR LNVLAHVLGK PYEIIFSEFQ HAPNKELVPS EGSIGINYGW SGDVKYHLGA
NKQIKDEHTV RAKVTLANNP SHLEFIDPIV EGYTRAAQEE RTEKGHPKQD VNKAMSILIH
GDAAFPGEGI VAETLNLNKL NGYQTGGTVH IIANNMIGFT TESRDSRSTK YASDLAKGYE
IPIVHVNADD PEACLAAVHI AMEYRNKFKS DFLIDLIGYR RFGHNEMDEP AMTQPKLYEK
VRKHPTVRKI YGNKLVNEGV LKSEELVKMN EEVQATLEKA YQKVPDKKVS QVHEIQLPEF
INSGLPKLKT SIDKKQLLKL NEELVNWPED FKVFPKLKRI LEKRAKALSE EGKVEWALGE
ALAFASLLED GTPIRITGQD SQRGTFAQRH IVLHDVETGD SYSPLHRLRD AKASFAVHNS
PLSEGSVLGF EYGYNVFAPE TLVLWEAQYG DFANAAQVFF DQFIAAGRAK WGQKSGLVML
LPHGFEGQGP EHSSGRLERF LQLAAEDSWQ VANLTNAAQY FHILRRQADL LKREEVRPLV
IMTPKSLLRN PQTVSPLSDL SEGEFKPVIE QPGLGQSPEK VKRLVLCSGK IAIDLTDKLN
SLEGNQDWVH ILRVEELYPF PKKIISSIIS KLTSLEEIVW VQEEPQNMGA WLFIDPKLRE
IAPQGVPVKY IGRRRRQSPA EGDPNIHRKD QNRIVTEALT WEKK
//
