Q6G1H9 (DAPE_BARQU) 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:	BQ00460

Organism

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

Taxonomic identifier

283165 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella › Bartonella quintana

Protein attributes

Sequence length	390 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 – 390	390	Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690		PRO_0000375471
Sites
	Active site	76	1	By similarity
	Active site	140	1	Proton acceptor By similarity
	Metal binding	74	1	Cobalt or zinc 1 By similarity
	Metal binding	107	1	Cobalt or zinc 1 By similarity
	Metal binding	107	1	Cobalt or zinc 2 By similarity
	Metal binding	141	1	Cobalt or zinc 2 By similarity
	Metal binding	169	1	Cobalt or zinc 1 By similarity
	Metal binding	363	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G1H9 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 72EAC2B4C5C0EF23	FASTA	390	42,837
	10 20 30 40 50 60 MPVLTDPLQL LQALIRCPSV TPYEAGALST LEQILTKMGF NVKRPVFTDK NTEDVENLYA 70 80 90 100 110 120 KMGGEGRHLM FAGHTDVVPP GALEDWTYPP FEGVIDQGKL YGRGAVDMKG GIACFVAALA 130 140 150 160 170 180 RILEKRSIKG MVSLLITGDE EGPALNGTVK LLKWAEQKGE KWTAALVGEP TSVKTVGDVI 190 200 210 220 230 240 KIGRRGSLSG VVTVKGRQGH VAFPERAANP LPLAGKLIQA LTQTALDRGT ENFQPSNLEL 250 260 270 280 290 300 TTIDTDNPAV NVIPAQTTIR FNIRYNDVWT KETLMTEIEK RLASVQLKNN DYQYPYYQLE 310 320 330 340 350 360 WIPSLGSVFI TKNDKLIKTL SNAIESVTGN IPEYSTSGGT SDARFIKDYC PVVEFGLPGQ 370 380 390 TMHMVDECVT LDAIETLTSV YERFIVDFFA

References

[1]

"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX897700 Genomic DNA. Translation: CAF25553.1.
RefSeq	YP_031772.1. NC_005955.1.
3D structure databases
ProteinModelPortal	Q6G1H9.
ModBase	Search...
Protein-protein interaction databases
STRING	283165.BQ00460.
Protein family/group databases
MEROPS	M20.010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAF25553; CAF25553; BQ00460.
GeneID	2867597.
KEGG	bqu:BQ00460.
PATRIC	31951219. VBIBarQui58630_0053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HOG000243770.
KO	K01439.
OMA	WDAPRLE.
ProtClustDB	PRK13009.
Enzyme and pathway databases
BioCyc	BQUI283165:GHZA-256-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. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPE_BARQU

Accession

Primary (citable) accession number: Q6G1H9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program