Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).By similarity

Catalytic activityi

Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi: L-lysine degradation via saccharopine pathway

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:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei372Sequence analysis1
Active sitei376Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyciRPRO272947:G1GT0-182-MONOMER
UniPathwayiUPA00868; UER00840

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
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
OrganismiRickettsia prowazekii (strain Madrid E)
Taxonomic identifieri272947 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
Proteomesi
  • UP000002480 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622691 – 401Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexAdd BLAST401

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotation1

Proteomic databases

PRIDEiQ9ZDY4

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

STRINGi272947.RP179

Structurei

3D structure databases

ProteinModelPortaliQ9ZDY4
SMRiQ9ZDY4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini115 – 152Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA
HOGENOMiHOG000281563
KOiK00658
OMAiMKVPSPG

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01347 sucB, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

Q9ZDY4-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:401
Mass (Da):43,979
Last modified:May 1, 1999 - v1
Checksum:i353F81339C5E9F23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235270 Genomic DNA Translation: CAA14646.1
PIRiG71728
RefSeqiNP_220569.1, NC_000963.1
WP_004595915.1, NC_000963.1

Genome annotation databases

EnsemblBacteriaiCAA14646; CAA14646; CAA14646
GeneIDi883874
KEGGirpr:RP179
PATRICifig|272947.5.peg.184

Entry informationi

Entry nameiODO2_RICPR
AccessioniPrimary (citable) accession number: Q9ZDY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 23, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Rickettsia prowazekii
    Rickettsia prowazekii (strain Madrid E): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health