Q6LAN3 (DAPEL_LISIV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: N-acetyldiaminopimelate deacetylase EC=3.5.1.47
Organism	Listeria ivanovii
Taxonomic identifier	1638 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate By similarity. HAMAP-Rule MF_01692
Catalytic activity	N-acetyl-LL-2,6-diaminoheptanedioate + H2O = acetate + LL-2,6-diaminoheptanedioate. HAMAP-Rule MF_01692
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (acetylase route): step 3/3. HAMAP-Rule MF_01692
Sequence similarities	Belongs to the peptidase M20A family. N-acetyldiaminopimelate deacetylase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Molecular function	Hydrolase
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
Molecular_function	N-acetyldiaminopimelate deacetylase activity 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 – 372	372	N-acetyldiaminopimelate deacetylase HAMAP-Rule MF_01692		PRO_0000376772
Sites
	Active site	69	1	By similarity
	Active site	128	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6LAN3 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E8147EE5E1581CAC	FASTA	372	41,470
	10 20 30 40 50 60 MDLNQFISIR RELHQIPETG YKEWKTQAYL LDYINKLPSR YLEVKKWRTG LLVRVSGTSP 70 80 90 100 110 120 TKTIGYRTDI DALPITEETG LAFESKHAGN MHACGHDLHM SIALGVLTHF ASKPAKDNLL 130 140 150 160 170 180 FVFQPAEEGP GGAKPIMESA EFAEWRPDSI YGLHIAPEYK VGQIAIKPGL LFANTSELFI 190 200 210 220 230 240 SFKGKGGHAA YPHLANDMVV AASAFVGQMQ TIISRNIDPM DSAVITIGRI HGGEIQNVIA 250 260 270 280 290 300 ETAFLDGTIR TLSPETMEIV WTRLKQLAKG WEEAYQCEVT FHAGSDYYQV DNDPAETAAF 310 320 330 340 350 360 IDFLKESYPK SYVPAKSAMT GEDFGYFLSG IKGFMFWLGV DSEYSLHHAK LNPKEEAIPF 370 AIEVLIHFLE SK

References

[1]	Dominguez G. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 19119 / DSM 20750 / JCM 7681 / NCTC 11846 / SLCC 2379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98994 Genomic DNA. Translation: CAC79603.1.
3D structure databases
ProteinModelPortal	Q6LAN3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00034; UER00024.
Family and domain databases
Gene3D	3.30.70.360. 1 hit.
HAMAP	MF_01692. DapEL.
InterPro	IPR023905. AcetylDAP_deacetylase. IPR017439. Amidohydrolase. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMs	TIGR01891. amidohydrolases. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. False negative. PS00759. ARGE_DAPE_CPG2_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPEL_LISIV

Accession

Primary (citable) accession number: Q6LAN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program