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Database: UniProt
Entry: I4WD39_9GAMM
LinkDB: I4WD39_9GAMM
Original site: I4WD39_9GAMM 
ID   I4WD39_9GAMM            Unreviewed;       119 AA.
AC   I4WD39;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Dihydrolipoamide succinyltransferase {ECO:0000313|EMBL:EIL97380.1};
DE            EC=2.3.1.61 {ECO:0000313|EMBL:EIL97380.1};
DE   Flags: Fragment;
GN   ORFNames=UU5_05376 {ECO:0000313|EMBL:EIL97380.1};
OS   Rhodanobacter sp. 115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL97380.1, ECO:0000313|Proteomes:UP000004557};
RN   [1] {ECO:0000313|EMBL:EIL97380.1, ECO:0000313|Proteomes:UP000004557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=115 {ECO:0000313|EMBL:EIL97380.1,
RC   ECO:0000313|Proteomes:UP000004557};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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:EIL97380.1}.
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DR   EMBL; AJXS01000133; EIL97380.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4WD39; -.
DR   Proteomes; UP000004557; Unassembled WGS sequence.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:EIL97380.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Transferase {ECO:0000313|EMBL:EIL97380.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          81..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         119
FT                   /evidence="ECO:0000313|EMBL:EIL97380.1"
SQ   SEQUENCE   119 AA;  12170 MW;  C1E90655846E82CB CRC64;
     MSTEVKVPVL PESVSDATIA TWYKKVGEAV KRDENLVDLE TDKVVLEVPS PVDGVLKEIR
     QESGATVNSQ EVIAVIEEGA AASAPAPAAK DEPKAAAPAP AAAKAEAPKA AAGVDELSP
//
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