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UniProtKB - P16263 (ODO2_BACSU)
Protein
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene
odhB
Organism
Bacillus subtilis (strain 168)
Status
Functioni
E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO2.
By similarityCatalytic activityi
- (R)-N6-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N6-(S8-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoABy similarityEC:2.3.1.61By similarity
Cofactori
(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity
: L-lysine degradation via saccharopine pathway Pathwayi
This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine. This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 388 | By similarity | 1 | |
Active sitei | 392 | By similarity | 1 |
GO - Molecular functioni
- dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
- tricarboxylic acid cycle Source: UniProtKB-KW
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Tricarboxylic acid cycle |
Enzyme and pathway databases
BioCyci | BSUB:BSU19360-MONOMER |
BRENDAi | 2.3.1.61, 658 |
UniPathwayi | UPA00868;UER00840 |
Names & Taxonomyi
Protein namesi | Recommended name: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61By similarity)Alternative name(s): 2-oxoglutarate dehydrogenase complex component E2 Short name: OGDC-E2 Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex |
Gene namesi | Name:odhB Synonyms:citM Ordered Locus Names:BSU19360 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162256 | 1 – 417 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexAdd BLAST | 417 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 42 | N6-lipoyllysinePROSITE-ProRule annotation | 1 |
Proteomic databases
jPOSTi | P16263 |
PaxDbi | P16263 |
PRIDEi | P16263 |
Interactioni
Subunit structurei
Forms a 24-polypeptide structural core with octahedral symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3).
By similarityProtein-protein interaction databases
STRINGi | 224308.BSU19360 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 76 | Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST | 76 | |
Domaini | 123 – 160 | Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST | 38 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 75 – 191 | DisorderedSequence analysisAdd BLAST | 117 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 91 – 107 | Basic and acidic residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 166 – 187 | Polar residuesSequence analysisAdd BLAST | 22 |
Sequence similaritiesi
Belongs to the 2-oxoacid dehydrogenase family.Curated
Keywords - Domaini
LipoylPhylogenomic databases
eggNOGi | COG0508, Bacteria |
InParanoidi | P16263 |
OMAi | MKVPSPG |
PhylomeDBi | P16263 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 4.10.320.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR036625, E3-bd_dom_sf IPR004167, PSBD IPR011053, Single_hybrid_motif IPR006255, SucB |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 1 hit PF02817, E3_binding, 1 hit |
SUPFAMi | SSF47005, SSF47005, 1 hit SSF51230, SSF51230, 1 hit |
TIGRFAMsi | TIGR01347, sucB, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 1 hit PS00189, LIPOYL, 1 hit PS51826, PSBD, 1 hit |
i Sequence
Sequence statusi: Complete.
P16263-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAEIKVPELA ESISEGTIAQ WLKQPGDYVE QGEYLLELET DKVNVELTAE
60 70 80 90 100
ESGVLQEVLK DSGDTVQVGE IIGTISEGAG ESSAPAPTEK TESKESVKEE
110 120 130 140 150
KQAEPAAQEV SEEAQSEAKS RTIASPSARK LAREKGIDLS QVPTGDPLGR
160 170 180 190 200
VRKQDVEAYE KPASKPAPQQ KQQPQAQKAQ QSFDKPVEVQ KMSRRRQTIA
210 220 230 240 250
KRLVEVQQTS AMLTTFNEVD MTAVMNLRKR RKDQFFEQNE VKLGFMSFFT
260 270 280 290 300
KAVVAALKKY PLLNAEIQGD ELIVKKFYDI GIAVAADEGL VVPVVRDADR
310 320 330 340 350
LTFAGIEKEI GELAKKARNN KLTLSELQGG SFTITNGGTF GSLMSTPILN
360 370 380 390 400
SPQVGILGMH KIQLRPVAID EERFENRPMM YIALSYDHRI VDGKEAVGFL
410
VTIKNLLEDP EQLLLEG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 287 | D → V in AAA22629 (PubMed:2500417).Curated | 1 | |
Sequence conflicti | 328 | Q → E in AAA22629 (PubMed:2500417).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27141 Genomic DNA Translation: AAA22629.1 AL009126 Genomic DNA Translation: CAB13828.2 |
PIRi | B32879 |
RefSeqi | NP_389818.2, NC_000964.3 WP_004399364.1, NZ_JNCM01000036.1 |
Genome annotation databases
EnsemblBacteriai | CAB13828; CAB13828; BSU_19360 |
GeneIDi | 939505 |
KEGGi | bsu:BSU19360 |
PATRICi | fig|224308.179.peg.2117 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27141 Genomic DNA Translation: AAA22629.1 AL009126 Genomic DNA Translation: CAB13828.2 |
PIRi | B32879 |
RefSeqi | NP_389818.2, NC_000964.3 WP_004399364.1, NZ_JNCM01000036.1 |
3D structure databases
SMRi | P16263 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU19360 |
Proteomic databases
jPOSTi | P16263 |
PaxDbi | P16263 |
PRIDEi | P16263 |
Genome annotation databases
EnsemblBacteriai | CAB13828; CAB13828; BSU_19360 |
GeneIDi | 939505 |
KEGGi | bsu:BSU19360 |
PATRICi | fig|224308.179.peg.2117 |
Phylogenomic databases
eggNOGi | COG0508, Bacteria |
InParanoidi | P16263 |
OMAi | MKVPSPG |
PhylomeDBi | P16263 |
Enzyme and pathway databases
UniPathwayi | UPA00868;UER00840 |
BioCyci | BSUB:BSU19360-MONOMER |
BRENDAi | 2.3.1.61, 658 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 4.10.320.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR036625, E3-bd_dom_sf IPR004167, PSBD IPR011053, Single_hybrid_motif IPR006255, SucB |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 1 hit PF02817, E3_binding, 1 hit |
SUPFAMi | SSF47005, SSF47005, 1 hit SSF51230, SSF51230, 1 hit |
TIGRFAMsi | TIGR01347, sucB, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 1 hit PS00189, LIPOYL, 1 hit PS51826, PSBD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ODO2_BACSU | |
Accessioni | P16263Primary (citable) accession number: P16263 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | July 7, 2009 | |
Last modified: | June 2, 2021 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families