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C6AB71 (C6AB71_BARGA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. 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 EMBL ACS50438.1
Ordered Locus Names:Bgr_00500 EMBL ACS50438.1
OrganismBartonella grahamii (strain as4aup) [Complete proteome] [HAMAP] EMBL ACS50438.1
Taxonomic identifier634504 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella ›

Protein attributes

Sequence length390 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 SAAS SAAS005941

Catalytic activity

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

Cofactor

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

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

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 SAAS SAAS005941

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01690 SAAS SAAS005941

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 site1401Proton 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 binding1411Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690
Metal binding1691Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690
Metal binding3631Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690

Sequences

Sequence LengthMass (Da)Tools
C6AB71 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: CCB7970CDACE072D

FASTA39042,782
        10         20         30         40         50         60 
MPVLTDPLQL LQRLIRCPSV TPHEAGALST LEQFLKKMGF HVERPIFTDK NTDNVENLYA 

        70         80         90        100        110        120 
KMGNEGPHLM FAGHTDVVPP GALDEWTYSP FEAVIDQGKL YGRGAVDMKG GIACFIAALA 

       130        140        150        160        170        180 
RVLEKRSIKG MVSFLITGDE EGPAVNGTVK LLKWAEKKGE KWTAALVGEP TSVKTVGDVI 

       190        200        210        220        230        240 
KIGRRGSISG IITVRGRQGH VAFPERAANP LPLASKLIQA LTQTALDKGT EDFQPSNLEL 

       250        260        270        280        290        300 
TSIDTGNLAV NVIPAQTTVH FNIRYNDLWT KETLMEEIKK RLALVQSKNN GDQYPSYQLE 

       310        320        330        340        350        360 
WIPSLGDVFL TKNDKLIQTL SNAIKSVTGN IPECSTSGGT SDARFIKDYC PVVEFGLPGQ 

       370        380        390 
TMHMVDECVA LDAVETLTTI YERFIVDFFA

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References

[1]"Run-off replication of host-adaptability genes is associated with gene transfer agents in the genome of mouse-infecting Bartonella grahamii."
Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F., Eriksson A.-S., Naslund K., Holmberg M., Lindroos H., Andersson S.G.E.
PLoS Genet. 5:e1000546-e1000546(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: as4aup.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001562 Genomic DNA. Translation: ACS50438.1.
RefSeqYP_002971115.1. NC_012846.1.

3D structure databases

ProteinModelPortalC6AB71.
ModBaseSearch...

Protein-protein interaction databases

STRING634504.Bgr_00500.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS50438; ACS50438; Bgr_00500.
GeneID7997026.
KEGGbgr:Bgr_00500.
PATRIC20539180. VBIBarGra67450_0053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243770.
KOK01439.
OMAWDAPRLE.
ProtClustDBPRK13009.

Enzyme and pathway databases

BioCycBGRA634504:GJI6-50-MONOMER.
UniPathwayUPA00034; UER00021.

Family and domain databases

HAMAPMF_01690. DapE.
InterProIPR001261. ArgE/DapE_CS.
IPR010182. DapE_ArgE.
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.
TIGRFAMsTIGR01910. DapE-ArgE. 1 hit.
TIGR01246. dapE_proteo. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6AB71_BARGA
AccessionPrimary (citable) accession number: C6AB71
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info