We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback.
Take me to UniProt BETA
UniProtKB - Q9JYL2 (DAPE_NEIMB)
Protein
Succinyl-diaminopimelate desuccinylase
Gene
dapE
Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
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.
By similarityCatalytic activityi
- EC:3.5.1.18
Cofactori
Zn2+UniRule annotation, Co2+UniRule annotationNote: Binds 2 Zn2+ or Co2+ ions per subunit.UniRule annotation
: L-lysine biosynthesis via DAP pathway Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route). 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 68 | Zinc 1By similarity | 1 | |
Active sitei | 70 | By similarity | 1 | |
Metal bindingi | 101 | Zinc 1By similarity | 1 | |
Metal bindingi | 101 | Zinc 2By similarity | 1 | |
Active sitei | 135 | Proton acceptorBy similarity | 1 | |
Metal bindingi | 136 | Zinc 2By similarity | 1 | |
Metal bindingi | 164 | Zinc 1By similarity | 1 | |
Metal bindingi | 350 | Zinc 2By similarity | 1 |
GO - Molecular functioni
- acetylornithine deacetylase activity Source: GO_Central
- cobalt ion binding Source: UniProtKB-UniRule
- succinyl-diaminopimelate desuccinylase activity Source: UniProtKB-UniRule
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- arginine biosynthetic process Source: GO_Central
- diaminopimelate biosynthetic process Source: UniProtKB-UniRule
- lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniRule
Keywordsi
Molecular function | Hydrolase |
Biological process | Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis |
Ligand | Cobalt, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.5.1.18, 3593 |
UniPathwayi | UPA00034;UER00021 |
Names & Taxonomyi
Protein namesi | Recommended name: Succinyl-diaminopimelate desuccinylase (EC:3.5.1.18)Short name: SDAP desuccinylase Alternative name(s): N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase |
Gene namesi | Name:dapE Ordered Locus Names:NMB1530 |
Organismi | Neisseria meningitidis serogroup B (strain MC58) |
Taxonomic identifieri | 122586 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000375624 | 1 – 381 | Succinyl-diaminopimelate desuccinylaseAdd BLAST | 381 |
Proteomic databases
PaxDbi | Q9JYL2 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
STRINGi | 122586.NMB1530 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | Q9JYL2 |
SMRi | Q9JYL2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9JYL2 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | CLU_021802_4_0_4 |
OMAi | LNSHHDT |
Family and domain databases
HAMAPi | MF_01690, DapE, 1 hit |
InterProi | View protein in InterPro IPR036264, Bact_exopeptidase_dim_dom IPR005941, DapE_proteobac IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
SUPFAMi | SSF55031, SSF55031, 1 hit |
TIGRFAMsi | TIGR01246, dapE_proteo, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9JYL2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTETQSLELA KELISRPSVT PDDRDCQKLL AERLHKIGFA AEELHFGDTK
60 70 80 90 100
NIWLRRGTKA PVVCFAGHTD VVPTGPVEKW DSPPFEPAER DGRLYGRGAA
110 120 130 140 150
DMKTSIACFV TACERFVAKH PNHQGSIALL ITSDEEGDAL DGTTKVVDVL
160 170 180 190 200
KARDELIDYC IVGEPTAVDK LGDMIKNGRR GSLSGNLTVK GKQGHIAYPH
210 220 230 240 250
LAINPVHTFA PALLELTQEV WDEGNEYFPP TSFQISNING GTGATNVIPG
260 270 280 290 300
ELNVKFNFRF STESTEAGLK QRVHAILDKH GVQYDLQWSC SGQPFLTQAG
310 320 330 340 350
KLTDVARAAI AETCGIEAEL STTGGTSDGR FIKAIAQELI ELGPSNATIH
360 370 380
QINENVRLND IPKLSAVYEG ILARLLAGNA V
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE002098 Genomic DNA Translation: AAF41885.1 |
PIRi | F81073 |
RefSeqi | NP_274537.1, NC_003112.2 WP_002225058.1, NC_003112.2 |
Genome annotation databases
EnsemblBacteriai | AAF41885; AAF41885; NMB1530 |
KEGGi | nme:NMB1530 |
PATRICi | fig|122586.8.peg.1942 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE002098 Genomic DNA Translation: AAF41885.1 |
PIRi | F81073 |
RefSeqi | NP_274537.1, NC_003112.2 WP_002225058.1, NC_003112.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1VGY | X-ray | 1.90 | A/B | 2-381 | [»] | |
4O23 | X-ray | 2.09 | A/B | 1-381 | [»] | |
4PPZ | X-ray | 2.00 | A | 1-381 | [»] | |
4PQA | X-ray | 1.78 | A | 1-381 | [»] | |
5UEJ | X-ray | 1.30 | A/B | 1-381 | [»] | |
AlphaFoldDBi | Q9JYL2 | |||||
SMRi | Q9JYL2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 122586.NMB1530 |
Proteomic databases
PaxDbi | Q9JYL2 |
Protocols and materials databases
DNASUi | 904046 |
Genome annotation databases
EnsemblBacteriai | AAF41885; AAF41885; NMB1530 |
KEGGi | nme:NMB1530 |
PATRICi | fig|122586.8.peg.1942 |
Phylogenomic databases
HOGENOMi | CLU_021802_4_0_4 |
OMAi | LNSHHDT |
Enzyme and pathway databases
UniPathwayi | UPA00034;UER00021 |
BRENDAi | 3.5.1.18, 3593 |
Miscellaneous databases
EvolutionaryTracei | Q9JYL2 |
Family and domain databases
HAMAPi | MF_01690, DapE, 1 hit |
InterProi | View protein in InterPro IPR036264, Bact_exopeptidase_dim_dom IPR005941, DapE_proteobac IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
SUPFAMi | SSF55031, SSF55031, 1 hit |
TIGRFAMsi | TIGR01246, dapE_proteo, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DAPE_NEIMB | |
Accessioni | Q9JYL2Primary (citable) accession number: Q9JYL2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 26, 2009 |
Last sequence update: | October 1, 2000 | |
Last modified: | May 25, 2022 | |
This is version 119 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families