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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Bartonella quintana (strain Toulouse) (Rochalimaea quintana)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei381 – 3811By similarity
Active sitei385 – 3851By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciBQUI283165:GHZA-1339-MONOMER.
RETL1328306-WGS:GSTH-3974-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:BQ13410
OrganismiBartonella quintana (strain Toulouse) (Rochalimaea quintana)
Taxonomic identifieri283165 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
ProteomesiUP000000597: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000162257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysinePROSITE-ProRule annotation

Proteomic databases

PRIDEiQ6FYD4.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi283165.BQ13410.

Structurei

3D structure databases

ProteinModelPortaliQ6FYD4.
SMRiQ6FYD4. Positions 181-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7776Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiFEKKHAV.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FYD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTGIRVPTL GESVTEATIG KWFKKLGEAV AVDEPLVELE TDKVTVEVPS
60 70 80 90 100
PVMGKLTEII AKEGDIVEVN AVLGFVESGA AGISQSFSPS ATSIPEAPSE
110 120 130 140 150
LEQSPSSSAT PSGTMPPAPS AAKLMAENNI AKSDISGSGK RGQILKEDVL
160 170 180 190 200
GALAQGTKAS TSVATLTASS SSAAPIQEMR EERVRMTKLR QTIARRLKDA
210 220 230 240 250
QNTAAMLTTF NEVDMSAVMD LRKRYKDLFE KKHGVKLGFM GFFTKAVCHA
260 270 280 290 300
LKEFPTVNAE IDGTDIVYKN YVNAGIAVGT DKGLVVPVVR DADQMSLAEI
310 320 330 340 350
EKEISRLGRL ARDGKLAVSD MQGGTFTITN GGVYGSLMST PILNAPQSGI
360 370 380 390 400
LGMHAIKERA MVVGGQIIIC PMMYLALSYD HRIVDGQEAV TFLVRVKESL
410
EDPERLVLDL
Length:410
Mass (Da):43,763
Last modified:July 19, 2004 - v1
Checksum:i216936AE2432DC05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41G → E in AAN78229 (PubMed:12874367).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY160680 Genomic DNA. Translation: AAN78229.2.
BX897700 Genomic DNA. Translation: CAF26799.1.
RefSeqiWP_011179953.1. NC_005955.1.
YP_032855.1. NC_005955.1.

Genome annotation databases

EnsemblBacteriaiCAF26799; CAF26799; BQ13410.
GeneIDi2866355.
KEGGibqu:BQ13410.
PATRICi31954159. VBIBarQui58630_1476.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY160680 Genomic DNA. Translation: AAN78229.2.
BX897700 Genomic DNA. Translation: CAF26799.1.
RefSeqiWP_011179953.1. NC_005955.1.
YP_032855.1. NC_005955.1.

3D structure databases

ProteinModelPortaliQ6FYD4.
SMRiQ6FYD4. Positions 181-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283165.BQ13410.

Proteomic databases

PRIDEiQ6FYD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF26799; CAF26799; BQ13410.
GeneIDi2866355.
KEGGibqu:BQ13410.
PATRICi31954159. VBIBarQui58630_1476.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiFEKKHAV.
OrthoDBiEOG610413.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
BioCyciBQUI283165:GHZA-1339-MONOMER.
RETL1328306-WGS:GSTH-3974-MONOMER.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the sucB gene encoding the immunogenic dihydrolipoamide succinyltransferase protein of Bartonella vinsonii subsp. berkhoffii and Bartonella quintana."
    Gilmore R.D. Jr., Carpio A.M., Kosoy M.Y., Gage K.L.
    Infect. Immun. 71:4818-4822(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC VR-358 / Fuller / CIP 107027.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Toulouse.

Entry informationi

Entry nameiODO2_BARQU
AccessioniPrimary (citable) accession number: Q6FYD4
Secondary accession number(s): Q8GCX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: March 4, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.