Succinyl-diaminopimelate desuccinylase - Escherichia coli O157:H7 (strain TW14359 / EHEC)

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C6UQ52 (C6UQ52_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended 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 ACT73177.1
Ordered Locus Names:	ECSP_3410 EMBL ACT73177.1

Organism

Escherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP] EMBL ACT73177.1

Taxonomic identifier

544404 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	375 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 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

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis HAMAP-Rule MF_01690 SAAS SAAS005941 Lysine biosynthesis HAMAP-Rule MF_01690 SAAS SAAS005941
Ligand	Cobalt HAMAP-Rule MF_01690 SAAS SAAS005941 Metal-binding HAMAP-Rule MF_01690 SAAS SAAS005941 Zinc HAMAP-Rule MF_01690 SAAS SAAS005941
Molecular function	Hydrolase HAMAP-Rule MF_01690 SAAS SAAS005941
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

Sites

Active site

By similarity HAMAP-Rule MF_01690

Active site

133

Proton acceptor By similarity HAMAP-Rule MF_01690

Metal binding

Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690

Metal binding

Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690

Metal binding

Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690

Metal binding

134

Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690

Metal binding

162

Cobalt or zinc 1 By similarity HAMAP-Rule MF_01690

Metal binding

348

Cobalt or zinc 2 By similarity HAMAP-Rule MF_01690

Sequences

Sequence

Length

Mass (Da)

Tools

C6UQ52 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: B249E6B09D84F2CA
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FASTA

375

41,241

        10         20         30         40         50         60 
MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAIGFTV ERMDFADTQN FWAWRGQGET 

        70         80         90        100        110        120 
LAFAGHTDVV PPGDADRWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPN 

       130        140        150        160        170        180 
HTGRLAFLIT SDEEASAHNG TVKAVEALMA RNERLDYCLV GEPSSIEVVG DVVKNGRRGS 

       190        200        210        220        230        240 
LTCNLTIHGV QGHVAYPHLA DNPVHRAAPF LNELVAIEWD QGNEFFPATS MQIANIQAGT 

       250        260        270        280        290        300 
GSNNVIPGEL FVQFNFRFST ELTDEMIKAQ VLALLEKHQL RYTVDWWLSG QPFLTARGKL 

       310        320        330        340        350        360 
VDAVVNAVEH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVNAADLQ 

       370 
LLARMYQRIM EQLVA

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References

[1]

"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K.

Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW14359 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001368 Genomic DNA. Translation: ACT73177.1.
RefSeq	YP_003079253.1. NC_013008.1.
3D structure databases
ProteinModelPortal	C6UQ52.
SMR	C6UQ52. Positions 2-374.
ModBase	Search...
Protein-protein interaction databases
STRING	544404.ECSP_3410.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACT73177; ACT73177; ECSP_3410.
GeneID	8217976.
KEGG	etw:ECSP_3410.
PATRIC	18390894. VBIEscCol9396_3464.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HOG000243770.
KO	K01439.
OMA	MWARRGN.
ProtClustDB	PRK13009.
Enzyme and pathway databases
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

C6UQ52_ECO5T

Accession

Primary (citable) accession number: C6UQ52

Entry history

Integrated into UniProtKB/TrEMBL:	September 22, 2009
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information