GenomeNet

Database: UniProt
Entry: A0A0B5ELJ0_STRA4
LinkDB: A0A0B5ELJ0_STRA4
Original site: A0A0B5ELJ0_STRA4 
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}.
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; 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
//
DBGET integrated database retrieval system