ID K6V222_9ACTN Unreviewed; 1267 AA.
AC K6V222;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:GAB90018.1};
GN Name=sucA {ECO:0000313|EMBL:GAB90018.1};
GN ORFNames=GORHZ_079_00110 {ECO:0000313|EMBL:GAB90018.1};
OS Gordonia rhizosphera NBRC 16068.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1108045 {ECO:0000313|EMBL:GAB90018.1, ECO:0000313|Proteomes:UP000008363};
RN [1] {ECO:0000313|EMBL:GAB90018.1, ECO:0000313|Proteomes:UP000008363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16068 {ECO:0000313|EMBL:GAB90018.1,
RC ECO:0000313|Proteomes:UP000008363};
RA Takarada H., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Ohji S., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia rhizosphera NBRC 16068.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00043700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004813}.
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:GAB90018.1}.
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DR EMBL; BAHC01000079; GAB90018.1; -; Genomic_DNA.
DR AlphaFoldDB; K6V222; -.
DR STRING; 1108045.GORHZ_079_00110; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000008363; Unassembled WGS sequence.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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 InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023213; CAT-like_dom_sf.
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; PF00198; 2-oxoacid_dh; 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; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008363};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 918..1116
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 828..855
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 73..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 138929 MW; 8DAFF33CA16514BE CRC64;
MYQQYKQDPS SVDPSWHEFL AGYEPGTNGA AEPAPATTTR PPAPRENATA APAPSAPVAG
TPAPAPTPAA STASAPAPKS PTSRASKPVT LDQQPAAPTP TRKAGPAKES TATKAASGHS
SASRDGSARS QKDRAPAKPP TPAAAGDESK VLRGPSAAIA KNMSASLEVP TATSVRAIPA
KLMIDNRIVV NNHLARTRGG KISFTHILGY ALVQAIKAFP NMNRHFAEVD GKPNVVTPAH
TNLGLAIDLV GKDGNRTLVV AAIKKCETMG FAEFYNAYQD IVRRARDGKL TAEDFSGVTI
SLTNPGTIGT VHSVPRLMKG QGAIIGAGAM EYPAEFQGAS DEQIAELGVG KLMTLTSTYD
HRIIQGAESG DFLRTVHELL LDDAFYDEIF TAFHIPYEPV RWRRDIPAGL VDKSTRVLEL
IAAYRSRGHL MADIDPLMMD SDARTSHPDL NVLTYGLTLW DLDRSFSVGG FHGEDKMKLR
DVLSVLRDAY CRHVGVEYTH ILEPEQQRWI QERVEVKHTK PPVAEQKYIL SKLNAAEAFE
TFLQTKYVGQ KRFSLEGAEA VIPMMDAVID QSAEHTLNEV VIGMPHRGRL NVLANIVGKP
YSKIFTEFEG NLNPSQAHGS GDVKYHLGAE GKYYQMFGDN EINVSLTANP SHLEAVDPVL
EGLVRAKQDL LDDDDQFSVL PLMLHGDAAF AGQGVVAETL NMAMLPGYRT GGTVHIVVNN
QVGFTTAPEH SRSTEYCTDV AKMIGAPIFH VNGDDPEACV WVAKLAVDYR AAFHKDVVID
LVCFRRRGHN EGDDPSMTQP AMYDVIDTKR GVRKSYTEAL IGRGDISTKE AEDALRDYQG
QLERVFNEVK ELEKYHPEPS PSVEQDQTLK TKLVTAVSKE VLESIGNAFL HVPDGFEPHP
RVKPVLERRH EMSRHGGIDW AFAELLAYGS LVLEGRTVRL SGQDSRRGTF TQRHSVLIDR
QSGSEYTPLN HLQLVDGSQG DGRFMVYDSP LSEFAVVGFE YGYSVGNPDA LVLWEGQFGD
FVNGAQSIID EFISSGEAKW GQLSDVVLLL PHGHEGQGPD HTSGRIERFL QLCAEGSMTV
ALPSTPASYF HLLRRHVLDG ISRPLIVFTP KSMLRNKAAV SPVKDFTDDK FRSVLDDPKF
VQGGDRSKVK RVLLVSGKLY YEMAARRDKE GRDDIAVVRI EQLYPVPHRR LRNTLEQYPN
AEDFAWVQEE PANQGPWPFL GLWLPEVLPD VLGGLRRISR RPMSAPSSGS SKVHAVEQRE
ILDEAFA
//
