ID A0A0Q9K2S2_9MICO Unreviewed; 1257 AA.
AC A0A0Q9K2S2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:KRE35526.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:KRE35526.1};
GN Name=kgd {ECO:0000313|EMBL:KRE35526.1};
GN ORFNames=ASG73_16460 {ECO:0000313|EMBL:KRE35526.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE35526.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE35526.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE35526.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE35526.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE35526.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE35526.1}.
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DR EMBL; LMRZ01000007; KRE35526.1; -; Genomic_DNA.
DR RefSeq; WP_055997930.1; NZ_LMRZ01000007.1.
DR AlphaFoldDB; A0A0Q9K2S2; -.
DR STRING; 1736393.ASG73_16460; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000051572; Unassembled WGS sequence.
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:KRE35526.1};
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 914..1107
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 37..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 138712 MW; 135C661A4400B776 CRC64;
MSLNDFGPNE WLVDELYEQF KNDRNSVDKA WWEFFENYTP GQSGGGNGTS AKGDSPASPQ
APAETKAAPA KSEPAKAAPA PAAKSEPKSA PAPAAKKPEP KAEPAKAAPA KAEPKDEAEE
PQDVLTPLRG VAARVVTNME ASLEVPVATS VRAIPAKLLI DNRIVINNHL KRSRGGKISF
THLIGYALIK ALREMPEMNV GFTTNDKGKP VVIQPAHIGL GIAIDLQKDD GTRQLMVPAI
KPAETMNFKD FWKAYEKVVG KARDGKLTVD DFQGTTMSLT NPGGIGTVHS IPRLMKGQGA
IIGVGALDYP AEWQGASTET LNRNAVSKLL TLTSTYDHRI IQGAQSGEFL RVVHQYLLGA
DGFYDEIFSS LRIPYEPVRW VQDISTTHDD DINKVARVQE LIHSYRVRGH LMADINPLEY
KQRHHSDLDI TTHGLTLWDL ERHFATGGFG GEPFLKLRKI LGILRDSYCR TTGVEYMHIQ
DPEQRRWMQE RVEVGYAKTT SDEQLRILRR LNAAEAFETF LQTKFVGQKR FSLEGGESVI
AVLDRILSRS AEEGMDEVCI GMPHRGRLNV LANIAGKSYG QIFREFEGQV DPRSVQGSGD
VKYHLGTEGE FTAESGDTTK VYLAANPSHL EAVNPVLEGI VRAKQDRLNH GGEDFPVLPI
LMHGDAAFAG QGVVAETLQQ SQLRGYRTGG TIHVVVNNQI GFTTSPNFSR SSVYSTDVAR
MIQAPIFHVN GDDPEACVRV AELAFEFRQK FHKDVVIDVV CYRRRGHNEG DDPSMTQPLM
YKLIESKRSV RKLYTESLIG RKDITTEEAD AALRDYQSQL ERVFVETKEA LKQSPDAASD
QPGSSDAPDN AGLERPAAQT SDKPIRSADE TAISETDLKH IGDMFDSPPA EFTIHPKLQQ
AMQKRAASVH DGGIDWGTGE MLAVGSLLMD GTPVRLTGQD TRRGTFVQRH AVLVDKSNGE
EWTPLNYLGG GQARFWVYDS LLSEYAAMGF EYGYSVERPD ALVLWEAQFG DFANGAATII
DEFISSSEQK WGQNSSVVLL LPHGYEGQGP DHSSARIERF LAMCAQENMT VAYPSTPASY
FHLLRRQAYH RPRRPLIVFT PKSMLRLKAA SSMPEDFTQG TFRAVLPDMT SPKGDDVTRV
LIAAGKVTWD LEAERKKRGD EQTAILHLER FYPLPGEALI TELAKYPNAD IVLVQEEPEN
QGAWPFLAMN LPADLAAHGE TRALRAVTRP PSASPAAGTA KKHAQEQAEL ISRAFDR
//
