B9KP62 (DAPE_RHOSK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinyl-diaminopimelate desuccinylase
Short name=SDAP desuccinylase
EC=3.5.1.18

Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase

Gene names

Name:	dapE
Ordered Locus Names:	RSKD131_2524

Organism

Rhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]

Taxonomic identifier

557760 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter › Rhodobacter sphaeroides

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls By similarity. HAMAP-Rule MF_01690
Catalytic activity	N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate. HAMAP-Rule MF_01690
Cofactor	Binds 1 Zn2+ ion per subunit By similarity. Binds 1 Co2+ ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. HAMAP-Rule MF_01690
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the peptidase M20A family. DapE subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Ligand	Cobalt Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP proteolysis Inferred from electronic annotation. Source: InterPro
Molecular_function	cobalt ion binding Inferred from electronic annotation. Source: HAMAP metallopeptidase activity Inferred from electronic annotation. Source: InterPro succinyl-diaminopimelate desuccinylase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690		PRO_0000375687
Sites
	Active site	71	1	By similarity
	Active site	135	1	Proton acceptor By similarity
	Metal binding	69	1	Cobalt or zinc 1 By similarity
	Metal binding	102	1	Cobalt or zinc 1 By similarity
	Metal binding	102	1	Cobalt or zinc 2 By similarity
	Metal binding	136	1	Cobalt or zinc 2 By similarity
	Metal binding	164	1	Cobalt or zinc 1 By similarity
	Metal binding	353	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	B9KP62 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: BD19DEE80B7D2F71	FASTA	380	40,404
	10 20 30 40 50 60 MPIDPVALTA DLVRCPSVTP EEGGALDLIE RILSGAGFDC TRVDRNGVPN LFARWGRKGA 70 80 90 100 110 120 NRTFGFNGHT DVVPVGDAAA WTRDPFGGEI ADGWLWGRGA TDMKSGVAAF VAAAVDFVQE 130 140 150 160 170 180 TPPDGAVVLT ITGDEEGDAA DGTVALLDWM AAEGEAMSVC LVGEPTCPER LGEMMKIGRR 190 200 210 220 230 240 GSMTAFFTAR GVQGHSAYPH RAKNPVAALA RLIDRLSSHD LDRGTEHFDA STLAVTTFDT 250 260 270 280 290 300 GNPATNVIPA LCRATVNIRF NDAHSGASLT RWLEEEAARV TAETGVEIAL SAKISGESFL 310 320 330 340 350 360 TPPGELSELV ARAVEAETGL RPEPSTSGGT SDARFVRAHC PVVEFGLVGK TMHQVDERVE 370 380 VGQIEPLKAI YLRILKDYFA

References

[1]	"Complete genome sequence of Rhodobacter sphaeroides KD131." Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K. J. Bacteriol. 191:1118-1119(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KD131 / KCTC 12085.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001150 Genomic DNA. Translation: ACM02384.1.
RefSeq	YP_002526885.1. NC_011963.1.
3D structure databases
ProteinModelPortal	B9KP62.
ModBase	Search...
Protein-protein interaction databases
STRING	557760.RSKD131_2524.
Protein family/group databases
MEROPS	M20.010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACM02384; ACM02384; RSKD131_2524.
GeneID	7359222.
KEGG	rsk:RSKD131_2524.
PATRIC	23184178. VBIRhoSph125910_3930.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HOG000243770.
KO	K01439.
OMA	WDAPRLE.
ProtClustDB	PRK13009.
Enzyme and pathway databases
BioCyc	RSPH557760:GH1P-2523-MONOMER.
UniPathway	UPA00034; UER00021.
Family and domain databases
HAMAP	MF_01690. DapE.
InterPro	IPR001261. ArgE/DapE_CS. IPR005941. DapE_proteobac. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMs	TIGR01246. dapE_proteo. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. False negative. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPE_RHOSK

Accession

Primary (citable) accession number: B9KP62

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program