ID A0A176KV98_9ACTN Unreviewed; 1272 AA.
AC A0A176KV98;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:OAA95903.1};
GN Name=kgd {ECO:0000313|EMBL:OAA95903.1};
GN ORFNames=A6P39_36755 {ECO:0000313|EMBL:OAA95903.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA95903.1};
RN [1] {ECO:0000313|EMBL:OAA95903.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA95903.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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:OAA95903.1}.
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DR EMBL; LWRP01000182; OAA95903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176KV98; -.
DR STRING; 710705.A6P39_36755; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
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 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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 139136 MW; 0751F5C85D130423 CRC64;
MSPQSPSNPS VSTDDQAGKN PAAAFGPNEW LVDEIYQQYL QDPNSVDRAW WDFFADYKPG
APATPAAAGT AAAGAAGTTS TAPQAQPAAP APQAAAPAPA APKPAAAPAP APAPAAQAAP
APAKPAQPAQ APAQPKPAAA KAAPAAAAPE GPELVTLRGP AAAVAKNMNA SLELPTATSV
RAVPVKLLFD NRIVINNHLK RARGGKISFT HLIGYAMVQA IKAMPSMNWS FGEKDGKPTL
VKPPHVNLGL AIDLVKPNGD RQLVVAAIKK AETLNFFEFW QAYEDIVRRA RDNKLTMDDF
TGVTVSLTNP GGLGTVHSVP RLMPGQSVIM GVGSMDYPAE FQGTSQDTLN KLGVSKVMTL
TSTYDHRVIQ GAASGEFLRA VANLLLGENG FYDDIFEALR IPYEPVRWLK DIDASHDDDV
TKAARVFELI HSYRVRGHVM ADTDPLEYRQ RKHPDLDIVE HGLTLWDLER EFAVGGFAGK
SMMKLRDILG VLRDSYCRTT GIEFMHIQDP KQRKWIQDRV ERGHSKPERE EQLRILRRLN
AAEAFETFLQ TKYVGQKRFS LEGGESVIPL LDAVIDSAAE SRLDEVVIGM AHRGRLNVLA
NIVGKSYAQI FREFEGNLDP KSMHGSGDVK YHLGAQGTFT GLDGEQITVS LAANPSHLET
VDPVIEGIAR AKQDIINKGG TDFTVLPVAI HGDAAFAGQG VVAETLNMSQ LRGYRTGGTV
HIVINNQVGF TAAPESSRSS MYATDVARMI EAPIFHVNGD DPEAVVRVAR LAFEFRQAFN
KDVVIDLICY RRRGHNESDN PAFTQPLMYD LIDKKRSVRK LYTESLIGRG DITLEEAEQA
LQDYQGQLEK VFTEVREAVT AQEGTGPVPD PQADFPVAVN TAISSEVVKR IAESQVNIPD
SFHVHPRLLP QLQRRATMVE DGTIDWGMGE TLAVGSLLLE GTPVRLSGQD SQRGTFGQRH
AVLIDRETGE EYTPLQYLAE EQARYNVYNS LLSEYAVMGF EYGYSLARPD ALVMWEAQFG
DFVNGAQTVV DEYISAAEQK WGQTSGVTLL LPHGYEGQGP DHSSARVERF LQLCAQNNMT
VAMPTLPSNY FHLLRWQVHN PHHKPLVVFT PKSMLRLKAA ASKTEEFTSG QFRPVIGDAT
VDPAAVRKVV FVAGKLYYDL EAERVKRGVT DTAIIRIERL YPLPGAELQA EVNKYPNAEK
YLWAQEEPAN QGAWPFIALN LIDHLDLAVG ADVPHGERLR RISRPHSSSP AVGSAKRHQA
EQEQLVREVF EA
//
