ID A0A1I3CJ59_9MICO Unreviewed; 1259 AA.
AC A0A1I3CJ59;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=E3O11_02065 {ECO:0000313|EMBL:TFB88840.1};
OS Cryobacterium levicorallinum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=995038 {ECO:0000313|EMBL:TFB88840.1, ECO:0000313|Proteomes:UP000297963};
RN [1] {ECO:0000313|EMBL:TFB88840.1, ECO:0000313|Proteomes:UP000297963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hh34 {ECO:0000313|EMBL:TFB88840.1,
RC ECO:0000313|Proteomes:UP000297963};
RA Liu Q., Xin Y.-H.;
RT "Genomics of glacier-inhabiting Cryobacterium strains.";
RL Submitted (MAR-2019) 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:TFB88840.1}.
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DR EMBL; SOFE01000003; TFB88840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3CJ59; -.
DR STRING; 995038.SAMN05216274_11366; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000297963; 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; 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; 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:TFB88840.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:TFB88840.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 921..1114
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1259 AA; 137927 MW; 569B70EB7A291F60 CRC64;
MSSQVTGGAS DETTSGEFGA NEWLVDELYE RFLIDKNLVD ESWWPVLESY NQTANTPIPA
DAAPAAAPAA SVSPAPAAPA AAAPAAVPAV PAAPAQVAEN QPTARTTSSA PKPAPVPADA
PVTSPQTVVT DESAPVKQDK VVPLRGMAKS LATNMVTSLT VPTATSVRTI PAKLLIDNRI
VMNNHMKRAR GGKVSFTHLI GWALIRALKM FPSQNVYYDE VDGKPSVVAP AHVGMGLAID
MPKPDGTRAL LVPAIKRADT MTFGEYLAAY EDLVTRARQN KLTADDFAGA TLSLTNPGGI
GTVHSVPRLM KGQGCIIGAG ALDYPAEFQG SSVKTLTGLA ISKTITLTST YDHRVIQGAG
SGEFLKIVHE LLIGQHNFYE EIFSALRIPY DPIHWAPDIS VDLASAVDKT ARVQELINSF
RVRGHLMADI DPLEYSQRSH PDLDIATHGL TFWDLDRSFV TGGFGAKRQM LLRDILGVLR
DSYCRTTGIE YMHIQDPAQR KWVQEKIEKS YVKPTHHEQM RILAKLNEAE AFETFLQTKY
VGQKRFSLEG GECTIPLLDT ILQGAAEQGL DEVAIGMAHR GRLNVLTNIA GKTYGEIFRE
FEGTQDPRTV HGSGDVKYHL GTTGMFRGED GAEIPVSLAA NPSHLEAGDG VLEGIVRAKQ
DRKPIGTFST LPILIHGDAA MAGQGVVLET LQMSQLRGYR TGGTVHIVVN NQLGFTTLPQ
DARTSVYATD VAKTIQAPIF HVNGDDPEAV VRAGELAFAY RQEFKKDVVV DLICYRRRGH
NEGDDPSMTQ PLMYNLVEAK RSVRKLYTEA LVGRGDITEE EYEAAHRDFQ DRLERAFLET
HAAQTASIPV ITPEMAATAK AEAEAQARED AAGEPETTGV PESVIQLIGD AFNNKPAGFT
VHNKLQQLLQ KRLDMSRNGN IDWSFGELLA LGSLLVEGTP VRFAGQDARR GTFVQRHAVL
HDRVNGQEWL PLANLKDNQA RFWIYDSLLS EYAAMGFEYG YSVERADALV LWEAQFGDFA
NGAQTIIDQF VSSAEQKWGQ RSSVVLLLPH GYEGQGPDHS SARIERFLQL CAEENMTVAR
PSTPASYFHL LRRQAYMRPR RPLIVFTPKS MLRLRGATSA VSELTSGKFE AVIDDARVND
KNAVKRVLFM AGKIYYDLLN ELEKNPNPEI ALVRVEQFYP LPAVELKNVA AQYPNAELAW
VQDEPENQGA WPFFYLETNK LGPRAIRLFS RPASASPAAG SAKRHAVEQA KLQREALTL
//
