Reviewed, UniProtKB/Swiss-Prot Q6FYD4 (ODO2_BARQU)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
      Short name=E2
    EC=2.3.1.61
Alternative name(s):
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene names

Name:	sucB
Ordered Locus Names:	BQ13410

Organism

Bartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]

Taxonomic identifier

803 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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 activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 410	410	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000162257
Regions
	Domain	2 – 76	75	Lipoyl-binding
Sites
	Active site	381	1	By similarity
	Active site	385	1	By similarity
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential
Experimental info
	Sequence conflict	4	1	G → E in AAN78229. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6FYD4-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 216936AE2432DC05	FASTA	410	43,763
	10 20 30 40 50 60 MTTGIRVPTL GESVTEATIG KWFKKLGEAV AVDEPLVELE TDKVTVEVPS PVMGKLTEII 70 80 90 100 110 120 AKEGDIVEVN AVLGFVESGA AGISQSFSPS ATSIPEAPSE LEQSPSSSAT PSGTMPPAPS 130 140 150 160 170 180 AAKLMAENNI AKSDISGSGK RGQILKEDVL GALAQGTKAS TSVATLTASS SSAAPIQEMR 190 200 210 220 230 240 EERVRMTKLR QTIARRLKDA QNTAAMLTTF NEVDMSAVMD LRKRYKDLFE KKHGVKLGFM 250 260 270 280 290 300 GFFTKAVCHA LKEFPTVNAE IDGTDIVYKN YVNAGIAVGT DKGLVVPVVR DADQMSLAEI 310 320 330 340 350 360 EKEISRLGRL ARDGKLAVSD MQGGTFTITN GGVYGSLMST PILNAPQSGI LGMHAIKERA 370 380 390 400 410 MVVGGQIIIC PMMYLALSYD HRIVDGQEAV TFLVRVKESL EDPERLVLDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12874367] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC VR-358 / Fuller / CIP 107027.
[2]	"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY160680 Genomic DNA. Translation: AAN78229.2. BX897700 Genomic DNA. Translation: CAF26799.1.
RefSeq	YP_032855.1.
3D structure databases
HSSP	HSSP built from PDB template 1E2O based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
GeneID	2866355.
GenomeReviews	Gene locus BQ13410 in contig BX897700_GR.
KEGG	bqu:BQ13410.
NMPDR	fig|283165.1.peg.1125.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6FYD4.
OMA	Q6FYD4. LTTYNEV.
Enzyme and pathway databases
BioCyc	BQUI283165:BQ13410-MON.
BRENDA	2.3.1.61. 292235.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. IPR006255. SucB. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_BARQU

Accession

Primary (citable) accession number: Q6FYD4
Secondary accession number(s): Q8GCX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)