A7ML10 (DAPE_CROS8) 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:	ESA_00778

Organism

Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]

Taxonomic identifier

290339 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Cronobacter › Cronobacter sakazakii

Protein attributes

Sequence length	375 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. HAMAP-Rule MF_01690 Binds 1 Co2+ ion per subunit By similarity. HAMAP-Rule MF_01690
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. HAMAP-Rule MF_01690
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 – 375	375	Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690		PRO_0000375548
Sites
	Active site	68	1	By similarity
	Active site	133	1	Proton acceptor By similarity
	Metal binding	66	1	Cobalt or zinc 1 By similarity
	Metal binding	99	1	Cobalt or zinc 1 By similarity
	Metal binding	99	1	Cobalt or zinc 2 By similarity
	Metal binding	134	1	Cobalt or zinc 2 By similarity
	Metal binding	162	1	Cobalt or zinc 1 By similarity
	Metal binding	348	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ML10 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 5F4EB07003167BEF	FASTA	375	41,244
	10 20 30 40 50 60 MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAVGFTV EPMNIGDTQN FWAWRGTGET 70 80 90 100 110 120 LAFAGHTDVV PAGDVERWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPH 130 140 150 160 170 180 HRGRLAFLIT SDEEASATNG TVKVVEALMA RGERLDYCLV GEPSSSEVVG DVVKNGRRGS 190 200 210 220 230 240 LTCNLTIHGV QGHVAYPHLA DNPVHRAAPM LNELVGIEWD RGNEFFPPTS MQIANIQAGT 250 260 270 280 290 300 GSNNVIPGDL HVQFNFRFST ELTDEMIKQR VVALLEKYQL RYTLDWWLSG QPFLTARGKL 310 320 330 340 350 360 VDAVVNAVHH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVKASDLQ 370 LLARMYQRIM EQLVA

References

[1]

"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species." Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J. PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-894.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000783 Genomic DNA. Translation: ABU76055.1.
RefSeq	YP_001436891.1. NC_009778.1.
3D structure databases
ProteinModelPortal	A7ML10.
SMR	A7ML10. Positions 4-374.
ModBase	Search...
Protein-protein interaction databases
STRING	290339.ESA_00778.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABU76055; ABU76055; ESA_00778.
GeneID	5550571.
KEGG	esa:ESA_00778.
PATRIC	20393765. VBICroSak107175_0690.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HOG000243770.
KO	K01439.
OMA	MWARRGN.
ProtClustDB	PRK13009.
Enzyme and pathway databases
BioCyc	CSAK290339:GJ80-772-MONOMER.
UniPathway	UPA00034; UER00021.
Family and domain databases
Gene3D	3.30.70.360. 1 hit.
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. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPE_CROS8

Accession

Primary (citable) accession number: A7ML10

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	October 2, 2007
Last modified:	May 29, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program