Reviewed, UniProtKB/Swiss-Prot P57389 (ODO2_BUCAI)

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:	BU303

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	420 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 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	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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000162259
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	391	1	Potential
	Active site	395	1	Potential
Amino acid modifications
	Modified residue	44	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	P57389-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: E0028D647A5CE34C	FASTA	420	48,092
	10 20 30 40 50 60 MKKINILVPD LPESISDATV VKWHKKIGDT VHCDDNIVDI ETDKVMLEVS SPCDGILQSI 70 80 90 100 110 120 LEKEGKVVIS QQTLGEINKS TVVDNHLSNN HIIEKEDNLL KKEEKYITTE EKKEIEYLLK 130 140 150 160 170 180 DNHKHLTPSM RRSVKIHNIN NGFLNQVIET SKKTNFENII KEEKKESNQI LFNHNIFNAN 190 200 210 220 230 240 ENNKNNNNKV TNRVKMTRLR QRIAERLLDS KNNTAMLTTF HEVNMKPIIL LRKKYGEDFE 250 260 270 280 290 300 KKHNVRIGFM SFFVKAVIQA LKNFPEINAY IDQTDIVFYK NFDISIAIST PRGLITPVIR 310 320 330 340 350 360 NADTMTMAEI EKKIKDFSIK GLQNKINIKE LMGGNFTITN GGVFGSLMST PIINPPQTAI 370 380 390 400 410 420 LGMHVIQERP VVVNGQIKIL PMMYLALSYD HRLIDGKESV GFLINIKNIL EDFNRIAIDV

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB13012.1.
RefSeq	NP_240126.1.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
GeneID	1110002.
GenomeReviews	Gene locus BU303 in contig BA000003_GR.
KEGG	buc:BU303.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57389.
OMA	P57389. INILVPD.
Enzyme and pathway databases
BioCyc	BSP107806:BU303-MON.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_BUCAI

Accession

Primary (citable) accession number: P57389

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 55 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)