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Q72AX3 (Q72AX3_DESVH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 SAAS SAAS001653

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 SAAS SAAS001653

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197 SAAS SAAS001653.

Sequence similarities

Belongs to the diaminopimelate epimerase family. HAMAP-Rule MF_00197

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region83 – 853Substrate binding By similarity HAMAP-Rule MF_00197
Region208 – 2092Substrate binding By similarity HAMAP-Rule MF_00197
Region219 – 2202Substrate binding By similarity HAMAP-Rule MF_00197

Sites

Active site831Proton donor/acceptor By similarity HAMAP-Rule MF_00197
Active site2181Proton donor/acceptor By similarity HAMAP-Rule MF_00197
Binding site181Substrate By similarity HAMAP-Rule MF_00197
Binding site531Substrate By similarity HAMAP-Rule MF_00197
Binding site741Substrate By similarity HAMAP-Rule MF_00197
Binding site1901Substrate By similarity HAMAP-Rule MF_00197
Site1581Important for catalytic activity By similarity HAMAP-Rule MF_00197
Site2081Important for catalytic activity By similarity HAMAP-Rule MF_00197

Amino acid modifications

Disulfide bond83 ↔ 218Size: 249-333 By similarity HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q72AX3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FC53A0F1844E88E4

FASTA28229,964
        10         20         30         40         50         60 
MSGKKATVPF HKLHGCGNDF VFIDNRHLKL SVEAMPDWAR SICRRAFGVG ADGLVFLDTA 

        70         80         90        100        110        120 
PQGHEADYIW HFYNADGSRA EMCGNASRCA AVLAVDLGFA GPRHAFGTDA GIVHAVADVE 

       130        140        150        160        170        180 
AGYAKVELTR PRDLAAGTTL ELEGTPFTVH FVNTGVPHAV VFSDSVDGLD LRRLGAALRY 

       190        200        210        220        230        240 
HPHFSPAGTN ANFASIIDRR TIHLRTYERG VEDETYACGT GAAATAFIAH TLGLTDASVG 

       250        260        270        280 
VRTSGGEVLG IDIEDGSIFL SGKAVRVFSG EMHPEGLGLT LP

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017285 Genomic DNA. Translation: AAS96343.1.
RefSeqYP_011084.1. NC_002937.3.

3D structure databases

ProteinModelPortalQ72AX3.
ModBaseSearch...

Protein-protein interaction databases

STRING882.DVU1867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS96343; AAS96343; DVU_1867.
GeneID2794311.
KEGGdvu:DVU1867.
PATRIC32063474. VBIDesVul119526_1710.

Phylogenomic databases

eggNOGCOG0253.
KOK01778.
OMAVPHLVGF.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycDVUL882:GJIL-1910-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

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

Entry information

Entry nameQ72AX3_DESVH
AccessionPrimary (citable) accession number: Q72AX3
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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