Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Succinyl-diaminopimelate desuccinylase

Gene

dapE

Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Zn2+UniRule annotationNote: Binds 1 Zn2+ ion per subunit.UniRule annotation
  • Co2+UniRule annotationNote: Binds 1 Co2+ ion per subunit.UniRule annotation

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 3 of the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route).UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (dapD)
  2. no protein annotated in this organism
  3. Succinyl-diaminopimelate desuccinylase (dapE)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route), the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi72Cobalt or zinc 1UniRule annotation1
Active sitei74UniRule annotation1
Metal bindingi105Cobalt or zinc 1UniRule annotation1
Metal bindingi105Cobalt or zinc 2UniRule annotation1
Active sitei139Proton acceptorUniRule annotation1
Metal bindingi140Cobalt or zinc 2UniRule annotation1
Metal bindingi168Cobalt or zinc 1UniRule annotation1
Metal bindingi354Cobalt or zinc 2UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis
LigandCobalt, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSAMA326297:G1G7Q-1735-MONOMER
UniPathwayiUPA00034; UER00021

Protein family/group databases

MEROPSiM20.010

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-diaminopimelate desuccinylaseUniRule annotation (EC:3.5.1.18UniRule annotation)
Short name:
SDAP desuccinylaseUniRule annotation
Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolaseUniRule annotation
Gene namesi
Name:dapEUniRule annotation
Ordered Locus Names:Sama_1647
OrganismiShewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Taxonomic identifieri326297 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000009175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003757251 – 382Succinyl-diaminopimelate desuccinylaseAdd BLAST382

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi326297.Sama_1647

Structurei

3D structure databases

ProteinModelPortaliA1S647
SMRiA1S647
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family. DapE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C9Y Bacteria
COG0624 LUCA
HOGENOMiHOG000243770
KOiK01439
OMAiLNSHHDT
OrthoDBiPOG091H059V

Family and domain databases

CDDicd03891 M20_DapE_proteobac, 1 hit
HAMAPiMF_01690 DapE, 1 hit
InterProiView protein in InterPro
IPR001261 ArgE/DapE_CS
IPR036264 Bact_exopeptidase_dim_dom
IPR005941 DapE_proteobac
IPR002933 Peptidase_M20
IPR011650 Peptidase_M20_dimer
PfamiView protein in Pfam
PF07687 M20_dimer, 1 hit
PF01546 Peptidase_M20, 1 hit
SUPFAMiSSF55031 SSF55031, 1 hit
TIGRFAMsiTIGR01246 dapE_proteo, 1 hit
PROSITEiView protein in PROSITE
PS00759 ARGE_DAPE_CPG2_2, 1 hit

Sequencei

Sequence statusi: Complete.

A1S647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPETHSDV IELTRELISR PSVTPLDEGC QDLMAKRLAA IGFTIEPMVF
60 70 80 90 100
EDTTNLWARR GTEGPVFCFA GHTDVVPVGD LNRWHTPPFD PVVIDGYIHG
110 120 130 140 150
RGAADMKGSL AAMVVAAERF VAEHPDHQGS IAFLITSDEE GPFINGTVRV
160 170 180 190 200
VETLEARHEK ITWALVGEPS STHLLGDVVK NGRRGSLTGN LTVKGIQGHV
210 220 230 240 250
AYPHLADNPI HRAAPALAEL SRIEWDKGNE FFPPTSFQIA NINGGTGASN
260 270 280 290 300
VIPGELKVMF NFRYSTEVTA ETLIARVLGI LDAHGLDYDI DWVFNGLPFL
310 320 330 340 350
TGEGPLLDAT REAIFEVTGT HTDPQTTGGT SDGRFIAPTG AQVIELGPVN
360 370 380
ATIHKVNECV KASDLELLTG CYQRILEKLL CN
Length:382
Mass (Da):41,367
Last modified:February 6, 2007 - v1
Checksum:iF819497CC2FF7B1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000507 Genomic DNA Translation: ABL99853.1
RefSeqiWP_011759761.1, NC_008700.1

Genome annotation databases

EnsemblBacteriaiABL99853; ABL99853; Sama_1647
KEGGisaz:Sama_1647

Similar proteinsi

Entry informationi

Entry nameiDAPE_SHEAM
AccessioniPrimary (citable) accession number: A1S647
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: February 6, 2007
Last modified: February 28, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health