Q89AJ6 (ODO2_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	sucB
Ordered Locus Names:	bbp_281

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
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 three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
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	L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway 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
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_0000162261
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	381	1	Potential
	Active site	385	1	Potential
Amino acid modifications
	Modified residue	44	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q89AJ6 [UniParc]. Last modified June 16, 2003. Version 1. Checksum: 224A816E151499B0	FASTA	410	46,543
	10 20 30 40 50 60 MNIINIFIPD LPESVTDATI IKWHKKKGDK VQEDTILVDI ETDKVILEIP SPSDGILNSI 70 80 90 100 110 120 IADKGKIVLP GQVIGTLLKI GIKNEEKIIK TTNNVVNTDN NQNINLKLLE KTYSPTVRRL 130 140 150 160 170 180 ISMHDLRDVD IIQGTGTKNR LTRKDILNYL KNIRSNTNKK INNYDLNAYN FNTTHKNHRS 190 200 210 220 230 240 IKRVKMTRLR KKISERLLST KNNTASLTTF NEVNMQSILN LRRKYGELFK QKHGIKLGLM 250 260 270 280 290 300 SFYVKAVIEA LKIFPEINAS IDNDEIIYYN YFDISIAIST PRGLVTPVLK NADLMSMAEI 310 320 330 340 350 360 EIKIKDFSEK GKNSKLTIDD LIGGNFTITN GGVFGSLFST PLINPPQSAI LGMHAIHKRP 370 380 390 400 410 VIVDENIEVH PMMYLALSYD HRLIDGKESV GFLLKIKEFL EDFSRIVLNI

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO27006.1.
RefSeq	NP_777901.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AJ6.
SMR	Q89AJ6. Positions 179-410.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO27006; AAO27006; bbp_281.
GeneID	1058259.
KEGG	bab:bbp281.
PATRIC	21245349. VBIBucAph80364_0277.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
KO	K00658.
OMA	ARMILEC.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-281-MONOMER.
UniPathway	UPA00868; UER00840.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	IPR003016. 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]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_BUCBP

Accession

Primary (citable) accession number: Q89AJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	June 16, 2003
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program