ID D7CHE7_STRBB Unreviewed; 1276 AA.
AC D7CHE7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:ADI07004.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:ADI07004.1};
GN Name=kgd {ECO:0000313|EMBL:ADI07004.1};
GN OrderedLocusNames=SBI_03883 {ECO:0000313|EMBL:ADI07004.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI07004.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI07004.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI07004.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002047; ADI07004.1; -; Genomic_DNA.
DR RefSeq; WP_014176478.1; NC_016582.1.
DR AlphaFoldDB; D7CHE7; -.
DR STRING; 749414.SBI_03883; -.
DR KEGG; sbh:SBI_03883; -.
DR PATRIC; fig|749414.3.peg.4021; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:ADI07004.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 928..1121
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 139461 MW; 258C24D7E0667122 CRC64;
MSPQSPNSSS VSTDQQDGQG SNPAAAFGPN EWLVDEIYQQ YLQDPNSVDR AWWDFFADYK
PGQDTSSAVA ESAPAPAAGG AAGTGAAAPA PVSNGAAPAP VKPAAPAVPP AAQQAAPAPA
PVKPAAPAPA AAPAKAAPAA KTAPAKAAEP AAPGAGPEYV TLRGPSAAVA KNMNASLQLP
TATSVRAVPV KLLFDNRIVI NNHLKRARGG KVSFTHLIGY AMVQALKAMP SMNHSFTEKD
GKPTLVKPEH INLGLAIDLV KPNGDRQLVV AAIKKAETLN FFEFWQAYED IVRRARANKL
TMEDFTGVTA SLTNPGGIGT VHSVPRLMPG QGLIIGVGAM EYPAEFQGTS QDTLNKLGIA
KVMTLTSTYD HRVIQGAASG EFLRIMSQLL LGENDFYDEI FKALRIPYEP VRWLRDIDVS
HDDDVTKAAR VFDLIHSYRV RGHVMADTDP LEYRQRKHPD LDIIEHGLTL WDLEREFAVG
GFAGKTMMNL RDILGVLRDS YCRTTGIEFM HIQDPKQRKW IQDRVERPHA KPERDEQLRI
LRRLNAAEAF ETFLQTKYVG QKRFSLEGGE SVIPLLDAVL DAAAESRLDE VVIGMAHRGR
LNVLANIVGK SYAQIFREFE GNLDPKSMHG SGDVKYHLGA EGTFTGLDGE QIAVSLTANP
SHLEAVDPVL EGVVRAKQDI IGKAGTDFTV LPVALHGDAA FAGQGVVAET LNMSQLRGYR
TGGTVHIVIN NQVGFTAAPA ASRSSMYATD VARMIEAPIF HVNGDDPEAV VRVARLAFEF
RQAFNKDVVI DLICYRRRGH NETDNPGFTQ PLMYDLIDKK RSVRKLYTES LIGRGDITLE
EAEQALQDFQ GQLEKVFTEV RDATSQPTPT AVPEPQPEFP VAVSTAVSQE IVKRIAESQV
NIPDRITVHP RLYPQLQRRA AMIEDDTIDW GMGETLAIGS LLMEGTPVRL AGQDSRRGTF
GQRHAVLVDR ETGEDYTPLL YLTDEQARYN VYDSLLSEYA AMGFEYGYSL ARPDALVMWE
AQFGDFVNGA QTIVDEFISS AEQKWGQTSG VTLLLPHGYE GQGPDHSSAR IERFLQLCGQ
NNMTVAAPTL PSNYFHLLRW QVHNPHHKPL VVFTPKSMLR LKAAASKTEE FLNGSFRPVI
GDETVDPAAV RKVVFTSGKV YYDLAAERDK RGLTDTAIIR LERLYPLPGA ELQAEIAKYS
GVQKFVWAQE EPANQGAWPF VALNLIDHLE LSVGADLPAS ERLVRVSRPH SSSPAVGSNK
RHQAEQQALV NEVLEI
//
