UniProtKB - Q9ZDY4 (ODO2_RICPR)
Protein
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene
sucB
Organism
Rickettsia prowazekii (strain Madrid E)
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 similarity
Catalytic 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.Proteins known to be involved in the 6 steps of the subpathway in this organism are:
- no protein annotated in this organism
- no protein annotated in this organism
- no protein annotated in this organism
- no protein annotated in this organism
- no protein annotated in this organism
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB)
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 | 372 | By similarity | 1 | |
Active sitei | 376 | 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 | RPRO272947:G1GT0-182-MONOMER |
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:sucB Ordered Locus Names:RP179 |
Organismi | Rickettsia prowazekii (strain Madrid E) |
Taxonomic identifieri | 272947 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162269 | 1 – 401 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexAdd BLAST | 401 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 43 | N6-lipoyllysinePROSITE-ProRule annotation | 1 |
Proteomic databases
PRIDEi | Q9ZDY4 |
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 | 272947.RP179 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 77 | Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST | 76 | |
Domaini | 115 – 152 | Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST | 38 |
Sequence similaritiesi
Belongs to the 2-oxoacid dehydrogenase family.Curated
Keywords - Domaini
LipoylPhylogenomic databases
eggNOGi | ENOG4105C7S Bacteria COG0508 LUCA |
HOGENOMi | HOG000281563 |
KOi | K00658 |
OMAi | MKVPSPG |
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.
Q9ZDY4-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSVKIIIPSL GESVTEATIA KWYKKLGDSV KTDELLLEIE TEKVTLEVNA
60 70 80 90 100
PCNGTIEKIA KTDGANVTVG EEIGEINEVV DTDTACTNNN SYKKQAIVQH
110 120 130 140 150
DSEQIVDKPA SSSNILAPSV QKLVTENKLD PNNIKGTGRG GRITKCDVLE
160 170 180 190 200
TINTTPVTIE TPALNKTNEE RTQRVRMSRL RKTIAQRLKD SQNTAAILTT
210 220 230 240 250
FNEIDMSKVI ALRNQYKEEF EKKHTVKLGF MSFFVKATIE ALKLIPSINA
260 270 280 290 300
EIDGDDLLYK NYYDIGVAVG TDQGLVVPVV RDADKMGFAD VEQAIGDLAK
310 320 330 340 350
KAREGKLSMS DLSGGTFSIS NGGVYGSLLS TPIINPPQSG ILGLHKTEER
360 370 380 390 400
AVVIDGKIEI RPMMYIALSY DHRIIDGKEG VSFLVKIKNL IENPEKLLLN
L
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ235270 Genomic DNA Translation: CAA14646.1 |
PIRi | G71728 |
RefSeqi | NP_220569.1, NC_000963.1 WP_004595915.1, NC_000963.1 |
Genome annotation databases
EnsemblBacteriai | CAA14646; CAA14646; CAA14646 |
GeneIDi | 883874 |
KEGGi | rpr:RP179 |
PATRICi | fig|272947.5.peg.184 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ235270 Genomic DNA Translation: CAA14646.1 |
PIRi | G71728 |
RefSeqi | NP_220569.1, NC_000963.1 WP_004595915.1, NC_000963.1 |
3D structure databases
SMRi | Q9ZDY4 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 272947.RP179 |
Proteomic databases
PRIDEi | Q9ZDY4 |
Genome annotation databases
EnsemblBacteriai | CAA14646; CAA14646; CAA14646 |
GeneIDi | 883874 |
KEGGi | rpr:RP179 |
PATRICi | fig|272947.5.peg.184 |
Phylogenomic databases
eggNOGi | ENOG4105C7S Bacteria COG0508 LUCA |
HOGENOMi | HOG000281563 |
KOi | K00658 |
OMAi | MKVPSPG |
Enzyme and pathway databases
UniPathwayi | UPA00868;UER00840 |
BioCyci | RPRO272947:G1GT0-182-MONOMER |
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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ODO2_RICPR | |
Accessioni | Q9ZDY4Primary (citable) accession number: Q9ZDY4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | May 1, 1999 | |
Last modified: | May 8, 2019 | |
This is version 119 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Rickettsia prowazekii
Rickettsia prowazekii (strain Madrid E): entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways