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Q9JV69 (DAPF_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diaminopimelate epimerase

Short name=DAP epimerase
EC=5.1.1.7
Gene names
Name:dapF
Ordered Locus Names:NMA0972
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan By similarity. HAMAP-Rule MF_00197

Catalytic activity

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. HAMAP-Rule MF_00197

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_00197

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197.

Sequence similarities

Belongs to the diaminopimelate epimerase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149855

Regions

Region11 – 122Substrate binding By similarity
Region76 – 783Substrate binding By similarity
Region215 – 2162Substrate binding By similarity
Region225 – 2262Substrate binding By similarity

Sites

Active site761Proton donor/acceptor By similarity
Active site2241Proton donor/acceptor By similarity
Binding site141Substrate By similarity
Binding site471Substrate By similarity
Binding site671Substrate By similarity
Binding site1641Substrate By similarity
Binding site1971Substrate By similarity
Site1661Important for catalytic activity By similarity
Site2151Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond76 ↔ 224 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q9JV69 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F7399BB2B5B56BED

FASTA28330,482
        10         20         30         40         50         60 
MNTLKFTKMH GLGNDFMVID AVSQDFTPED APIAAWADRF RGVGFDQLLV VGRSETEGVD 

        70         80         90        100        110        120 
FRYRIFNADG SEVGQCGNGA RCFARFVADK GLTDKKEICV ETANGVIFPK LSDNGMVTVN 

       130        140        150        160        170        180 
MGKPRFMPSE IPFVPESGEG DDACIYGVHL ESGIQPVSCV NMGNPHAVIV VDDVECAQVR 

       190        200        210        220        230        240 
ETGSLIEPHR QFPERVNVGF MQIVSRTAIR LRVFERGVGE TQACGTGACA AVVAGIRLGL 

       250        260        270        280 
LDEGKTVEVI LPGGTLYIEW ACGGDVMMTG PAETVFEGEL AYS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM08196.1.
PIRC81944.
RefSeqYP_002342394.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JV69.
SMRQ9JV69. Positions 4-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA0972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM08196; CAM08196; NMA0972.
GeneID906949.
KEGGnma:NMA0972.
PATRIC20362860. VBINeiMen132687_1139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKHINREQ.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-899-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689. PTHR31689. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPF_NEIMA
AccessionPrimary (citable) accession number: Q9JV69
Secondary accession number(s): A1IR12
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways