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G8T6D6 (G8T6D6_BRUAO) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 11. Feed History...

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

Protein namesRecommended name:
Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690
Short name=SDAP desuccinylase HAMAP-Rule MF_01690
EC=3.5.1.18 HAMAP-Rule MF_01690
Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase HAMAP-Rule MF_01690
Gene names
Name:dapE HAMAP-Rule MF_01690
ORF Names:BAA13334_II01762 EMBL AEW19669.1
OrganismBrucella abortus A13334 EMBL AEW19669.1
Taxonomic identifier1104320 [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. SAAS SAAS005941 HAMAP-Rule MF_01690

Catalytic activity

N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate. SAAS SAAS005941 HAMAP-Rule MF_01690

Cofactor

Binds 1 Co2+ ion per subunit By similarity. SAAS SAAS005941 HAMAP-Rule MF_01690

Binds 1 Zn2+ ion per subunit By similarity. SAAS SAAS005941 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. SAAS SAAS005941 HAMAP-Rule MF_01690

Subunit structure

Homodimer By similarity. SAAS SAAS005941 HAMAP-Rule MF_01690

Sequence similarities

Belongs to the peptidase M20A family. DapE subfamily. HAMAP-Rule MF_01690

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site761 By similarity HAMAP-Rule MF_01690
Active site1411Proton acceptor By similarity HAMAP-Rule MF_01690
Metal binding741Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding1071Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding1071Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690
Metal binding1421Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690
Metal binding1701Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding3681Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690

Sequences

Sequence LengthMass (Da)Tools
G8T6D6 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: E0B7B1F2BB0BE193

FASTA39542,895
        10         20         30         40         50         60 
MTLPVNPVDN LAALIRCPSV TPAEGGALTA LEKMLKLMGF SANRPVFSDD NTPDIENLYA 

        70         80         90        100        110        120 
RKSGNGPHLM FAGHTDVVPP GDEKDWKHPP FAAEIEDGVM 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]"Complete Genome Sequence of Brucella abortus A13334, a New Strain Isolated from the Fetal Gastric Fluid of Dairy Cattle."
Kim H., Jeong W., Jeoung H.Y., Song J.Y., Kim J.S., Beak J.H., Parisutham V., Lee S.K., Kim J.W., Kim J.Y., Jung S.C., Her M., An D.J.
J. Bacteriol. 194:5444-5444(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A13334 EMBL AEW19669.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003177 Genomic DNA. Translation: AEW19669.1.
RefSeqYP_005114573.1. NC_016777.1.

3D structure databases

ProteinModelPortalG8T6D6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW19669; AEW19669; BAA13334_II01762.
GeneID11684940.
KEGGbaa:BAA13334_II01762.

Phylogenomic databases

KOK01439.

Enzyme and pathway databases

BioCycBABO1104320:GKD4-3358-MONOMER.
UniPathwayUPA00034; UER00021.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
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 nameG8T6D6_BRUAO
AccessionPrimary (citable) accession number: G8T6D6
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: May 29, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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