ID A0A0B5ELJ0_STRA4 Unreviewed; 1276 AA.
AC A0A0B5ELJ0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:AJE82384.1};
GN ORFNames=SLNWT_2008 {ECO:0000313|EMBL:AJE82384.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE82384.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE82384.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001267};
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:ARBA00033664};
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}.
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DR EMBL; CP010519; AJE82384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5ELJ0; -.
DR STRING; 1888.Salbus254_1786; -.
DR KEGG; sals:SLNWT_2008; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000031523; Chromosome.
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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031523};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
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..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 140217 MW; A9F8C878724837EA CRC64;
MSPQSPSNST SPGLKPGGTP TTDQDGQGKN PAAAFGPNEW LVDEIYQQYL QDPNSVDRAW
WDFFADYKPG GGATQAKQTA APAAQAPAAP SAPAQAPAPA APAKPAQAAQ PAQAAPAAAA
PAKQAAPAAK PAAAPAKAAP AAKAKEEQPA AEAPAGPELV TLRGPSAAVA KNMNASLELP
TATSVRAVPV KLLFDNRIVI NNHLKRARGG KISFTHLIGY AMVQAIKAMP SMNYSFAQKD
GKPTLVKPEH VNLGLAIDLV KPNGDRQLVV AAIKAAETLN FFEFWQAYED IVRRARDNKL
TMDDFSGVTV SLTNPGGIGT VHSVPRLMPG QAVIMGVGAM EYPAEYQGTS QDTLNKLGIS
KVMTLTSTYD HRVIQGAASG EFLRNVANLL LGENDFYDEI FKSLRIPYEP VRWNRDIDAS
HDDDVTKAAR VFELIHSYRV RGHVMADTDP LEYMQRKHPD LDIAEHGLTL WDLEREFAVG
GFAGKTLMKL RDILGVLRDS YCRTTGIEFM HIQDPKQRKW IQDRIERPHS KPEREEQLRI
LRRLNSAEAF ETFLQTKYVG QKRFSLEGGE SVIPLLDAVL DSAAENRLDE VVIGMAHRGR
LNVLANIVGK SYAQIFREFE GNLDPKSMHG SGDVKYHLGA EGTFTGLDGE QIKVSLAANP
SHLETVDPVI EGISRAKQDI INKGGTDFTV LPVALHGDAA FAGQGVVAET LNMSQLRGYR
TGGTVHIVIN NQVGFTAAPE SSRSSMYATD VARMIEAPIF HVNGDDPEAV VRVARLAFEF
RQAFNKDVVI DLICYRRRGH NESDNPAFTQ PLMYDLIDKK RSVRKLYTES LIGRGDITLE
EAEQALQDFQ GQLEKVFTEV REAVSHPGEA HLPDPQAEFP VAVNTAISQE VVKRIAESQV
NIPERVTVHP RLLPQLQRRA AMVEDGTIDW GMGETLAVGS LLLEGVPVRL SGQDSRRGTF
GQRHGVLIDR ETGEDYTPLL YLSEDQARYN VYDSLLSEYA VMGFEYGYSL ARPESLVMWE
AQFGDFVNGA QTVVDEYISA AEQKWGQTSG VTLLLPHGYE GQGPDHSSAR IERFLQLCAQ
NNMTVAMPTL PSNYFHLLRW QVHNPHHKPL VVFTPKSMLR LKAAASKTEE FTSGQFRPVI
SDDSVDPSVV RKVVFCAGKL YYDLDAARKK REANDVAIIR LERLYPLPGT ELQAEIAKYP
NAEKYLWAQE EPANQGAWPF IALNLIDHLD LAVGADIPHG ERLRRISRPH SSSPAVGSAK
RHQAEQEQLV NEVFEA
//