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A5VVT7 (DAPE_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:BOV_A0972
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella ›

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690
PRO_0000375489

Sites

Active site761 By similarity
Active site1411Proton acceptor By similarity
Metal binding741Cobalt or zinc 1 By similarity
Metal binding1071Cobalt or zinc 1 By similarity
Metal binding1071Cobalt or zinc 2 By similarity
Metal binding1421Cobalt or zinc 2 By similarity
Metal binding1701Cobalt or zinc 1 By similarity
Metal binding3681Cobalt or zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VVT7 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 7DDBA8AB53F43B80

FASTA39542,809
        10         20         30         40         50         60 
MTLPVNPADN LAALIRCPSV TPAEGGALTA LEKMLKLMGF SANRPVFSDD NTPDIENLYA 

        70         80         90        100        110        120 
RKSGNGPHLM FAGHTDVVPP GDEKDWKHPP FAAAIEDGVM YGRGAVDMKG GIACFVAAVA 

       130        140        150        160        170        180 
RHIEKHGNIK GSISFLITGD EEGPAVNGTV KLLEWAKQRG ESWDASIVGE PTNPNALGDM 

       190        200        210        220        230        240 
IKIGRRGSLS GTITVHGVQG HAAYPHLAEN PVRGIVTLVD SLLYPAFDEG TANFQASNLE 

       250        260        270        280        290        300 
VTTIDVGNKA TNVIPNKATA SFNIRFNDTW TAESLQAEII SRLERAARDN RLRQGRETPI 

       310        320        330        340        350        360 
KYELTWRERP SHVFLTHDEK LIGTLTASVE AVTGKRPELS TSGGTSDARF IKDYCPVVEF 

       370        380        390 
GLTGQTMHMV DERVALADLE GLTQIYERFI ADFFG

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000709 Genomic DNA. Translation: ABQ62668.1.
RefSeqYP_001257942.1. NC_009504.1.

3D structure databases

ProteinModelPortalA5VVT7.
ModBaseSearch...

Protein-protein interaction databases

STRING444178.BOV_A0972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ62668; ABQ62668; BOV_A0972.
GeneID5204144.
KEGGbov:BOV_A0972.
PATRIC17859367. VBIBruOvi136990_1119.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243770.
KOK01439.
OMAWDAPRLE.
ProtClustDBPRK13009.

Enzyme and pathway databases

BioCycBOVI444178:GH2V-3074-MONOMER.
UniPathwayUPA00034; UER00021.

Family and domain databases

HAMAPMF_01690. DapE.
InterProIPR001261. ArgE/DapE_CS.
IPR005941. DapE_proteobac.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMSSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMsTIGR01246. dapE_proteo. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPE_BRUO2
AccessionPrimary (citable) accession number: A5VVT7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: July 10, 2007
Last modified: May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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