ID A0A0M4DHN8_STRPR Unreviewed; 1272 AA.
AC A0A0M4DHN8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:ALC20905.1};
DE SubName: Full=Multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit {ECO:0000313|EMBL:QMU16301.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:QMU16301.1};
GN ORFNames=H3L99_24005 {ECO:0000313|EMBL:QMU16301.1}, SPRI_2599
GN {ECO:0000313|EMBL:ALC20905.1};
OS Streptomyces pristinaespiralis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=38300 {ECO:0000313|EMBL:ALC20905.1};
RN [1] {ECO:0000313|EMBL:ALC20905.1, ECO:0000313|Proteomes:UP000060513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCCB 10218 {ECO:0000313|EMBL:ALC20905.1,
RC ECO:0000313|Proteomes:UP000060513};
RA Tian J., Yang J., Li L., Ruan L., Wei W., Zheng G., Wei Z., Yang S., Ge M.,
RA Jiang W., Lu Y.;
RT "Genome sequence of the pristinamycin over-producing bacterium Streptomyces
RT pristinaespiralis HCCB10218.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QMU16301.1, ECO:0000313|Proteomes:UP000514765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR11 {ECO:0000313|EMBL:QMU16301.1,
RC ECO:0000313|Proteomes:UP000514765};
RA Handel F., Kulik A., Mast Y.;
RT "Investigation of the effector binding capability of pristinamycin
RT transcriptional regulators.";
RL Submitted (JUL-2020) 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}.
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DR EMBL; CP011340; ALC20905.1; -; Genomic_DNA.
DR EMBL; CP059696; QMU16301.1; -; Genomic_DNA.
DR RefSeq; WP_053557736.1; NZ_CP059696.1.
DR AlphaFoldDB; A0A0M4DHN8; -.
DR STRING; 38300.SPRI_2599; -.
DR KEGG; spri:SPRI_2599; -.
DR PATRIC; fig|38300.4.peg.2742; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000060513; Chromosome.
DR Proteomes; UP000514765; 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: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:QMU16301.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 924..1117
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 139429 MW; D454E572C66CC4F2 CRC64;
MSSQSPSNSS ISTDQAGQGQ NPAAAFGANE WLVDEIYQQY LQDPNSVDRA WWDFFADYKP
GAAATADAPA AGAKQTQSDA AAVTAAAPAP AAAPARPETP AQPAPAAPAP AAPAAPAAQA
PAPAKAAPAA APAKPAAKPA PAAKADGSQA EGPEFVTLRG PAAAVAKNMN ASLELPTATS
VRAVPVKLLF DNRIVINNHL KRARGGKISF THLIGYAMVQ AIKAMPSMNW SFAEKDGKPT
LVKPDHVNFG LAIDLVKPNG DRQLVVAGIK KAETLNFFEF WQAYEDIVRR ARTNKLTMDD
FTGVTVSLTN PGGLGTVHSV PRLMPGQSVI MGVGSMDYPA EFQGTSQDTL NKLGISKVMT
LTSTYDHRVI QGAASGEFLR IVANFLLGEE GFYDEIFESL RIPYEPVRWL KDIDASHDDD
VTKAARVFEL IHSYRVRGHV MADTDPLEYR QRKHPDLDIT EHGLTLWDLE REFAVGGFAG
KSMMKLRDIL GVLRESYCRT TGIEFMHIQD PKQRKWLQDR VERAASKPER EEQLRILRRL
NAAEAFEIFL QTKYVGQKRF SLEGGESVIP LLDAVIDSAA ESRLDEVVIG MAHRGRLNVL
ANIVGKSYAQ IFREFEGNLD PKSMHGSGDV KYHLGAEGTF TGLDGEQIKV SLVANPSHLE
AVDPVLEGVS RAKQDVINKG GTDFTVLPIA LHGDAAFAGQ GVVAETLNMS QLRGYRTGGT
VHVVINNQVG FTAAPESSRS SMYATDVARM IEAPIFHVNG DDPEAVVRVA RLAFEFRQAF
NKDVVIDLIC YRRRGHNEGD NPSFTNPQMY NLIDKKRSVR KLYTESLIGR GDITLEEAEQ
SLQDFQGQLE KVFAEVREAT SHPAPAHVPD VEAEFPVAVN TAVSQEVVKR IAESQVNIPD
NITVHPRLMP QMQRRAASVE DGTIDWGMGE TLAIGSLLME GTPVRLSGQD TRRGTFGQRH
AVLVDQETGE DYTPLLYLSE DQARYNVYDS LLSEYAAMGF EYGYSLARPD ALVMWEAQFG
DFVNGAQTVV DEFISSAEQK WGQHSGVTLL LPHGYEGQGP DHSSARPERF LQMCAQDNMT
VAMPTLPSNY FHLLRWQVHN PHHKPLIVFT PKSMLRLKAA ASKVEEFTTG GFRPVIGDDS
VDPNAVRKVV FCSGKVYYDL EAEREKRGVT DTAIIRLERL YPLPGAEVQA EIAKYPNAEK
YLWTQEEPAN QGAWPFIALN LIDHLDLAVG ADIPHGERLR RISRPHSSSP AVGSAKRHQA
EQQQLVNEVF DA
//
