ID A0A1L7D408_9CORY Unreviewed; 1252 AA.
AC A0A1L7D408;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:APT92807.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:APT92807.1};
GN Name=kgd {ECO:0000313|EMBL:APT92807.1};
GN ORFNames=CPHO_07795 {ECO:0000313|EMBL:APT92807.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT92807.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT92807.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT92807.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-2014) 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; CP009249; APT92807.1; -; Genomic_DNA.
DR RefSeq; WP_075734691.1; NZ_VXKJ01000043.1.
DR AlphaFoldDB; A0A1L7D408; -.
DR STRING; 161895.CPHO_07795; -.
DR KEGG; cpho:CPHO_07795; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000185491; Chromosome.
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:APT92807.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000185491};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 899..1095
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 28..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 138651 MW; 3A86C33753B1DFF1 CRC64;
MRRASAVSNS NIFGPNAWLI DEQFQQYSED PNSVDKEWRE YFEANGAPKS PESSPAKDAA
TSPAAVKKTE GSTIAKKQQV RKTEVSEAAK ESKVTTEKSQ KKAAEKPARK DQPASPLDRI
GDAPKAGASQ LKGMFKAIAK NMDESLTIPT ATTVRDMPVK LMWENRALIN EHLKRTRGGK
ISFTHILGYA MVKASQIHPG MNVRYEEKDG KPHVVQPEHI NLGLAIDLPQ KDGSRALVVA
AIKECENKSF TEFIDAYEDI VNRSRKNKLT MDDFTGVTIN LTNPGGIGTR HSIARLTKGS
GAIIGVGSMD YPAEFAGASA DRLAELGVGR LVTMSSTYDH RVIQGAESGE YLRTLSQLIN
DDKFWDELFD SMQVPYQPFR WAQDVPNTGV NKDARVLQLI EAYRSRGHLL ANVNPLGWKQ
PGLPWPNHRD LDMQTYGLTI WDLDRSFKVG GFGHKESMTL REVLSRLRAA YTQKVGSEFM
HIMDRDEREW LRERLEAGRP KPTNAEQKYI LQKVNSAEAF ENFLGTKYVG QKRFSLEGAE
SMIPLMDAII DTAAGQGLKE AVIGMPHRGR LNVLFNIVGK PLADIFGEFD GNYKGGQQGG
SGDVKYHLGA EGEYLQMFGD GEINVTLAAN PSHLEAVNPV LEGLARAKED LIAEPGEHPV
IPITLHGDAS FAGLGVVQET INLSQLDAYT VGGTVHIVVN NQVGFTTTPD SGRSTFYATD
LAKGFDCPVF HVNGNDPEAV VWVGQLATEY RHKFGKDVFI DLICYRLRGH NEADDPSMTQ
PLLYDVIKDH KGVRESYTDE LIGRGDLSDA EAEAAARDFH DQMESVFADH KEAEEQAPRE
QFGITDSQEL PHGLDTSITA EELAALGQAY LDTPETFQYH KRVHKIAETR AKNAIEGGID
WGFGELVAFG SLANAGRHVR LVGEDSRRGT FTQRHAVAFD PTDAEEFNPL NELALKRGNG
GKFEVYNSAL TEFAGLGFEY GYTLGNEDAV VAWEAQFGDF ANGAQTIIDQ YISSGEAKWG
ELSSLILLLP HGYEGQGPDH SSARIERFLQ LCAEGSMTVA QPTTPANHFH LLRRQALGSL
KRPLVVITPK SMLRNKAATS PVEEFTEVPK FRSVINDPRF YDMFGNKLAE GDKVKTIMLV
SGKLYYDLEK KRADDGRDDI AIVRVEMLHP IPYNRLGEAF AAYPNAEQIR FVQDEPANQG
PWPFYNEHLP ELIPDMPKMV RVSRRAQSST ATGNTKVHAR EHEALLKEAF NV
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