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Q8F814 (DAPAT_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:
LL-diaminopimelate aminotransferase

Short name=DAP-AT
Short name=DAP-aminotransferase
Short name=LL-DAP-aminotransferase
EC=2.6.1.83
Gene names
Name:dapL
Ordered Locus Names:LA_0776
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli By similarity. HAMAP-Rule MF_01642

Catalytic activity

LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O. HAMAP-Rule MF_01642

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01642

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1. HAMAP-Rule MF_01642

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01642

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_0000342247

Sites

Binding site421Substrate; via amide nitrogen By similarity
Binding site721Pyridoxal phosphate; shared with dimeric partner By similarity
Binding site751Substrate; shared with dimeric partner By similarity
Binding site1091Substrate By similarity
Binding site1321Substrate By similarity
Binding site1871Pyridoxal phosphate By similarity
Binding site1871Substrate By similarity
Binding site2151Pyridoxal phosphate By similarity
Binding site2181Pyridoxal phosphate By similarity
Binding site2461Pyridoxal phosphate By similarity
Binding site2481Pyridoxal phosphate By similarity
Binding site2571Pyridoxal phosphate By similarity
Binding site2921Substrate; shared with dimeric partner By similarity
Binding site3881Substrate By similarity

Amino acid modifications

Modified residue2491N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8F814 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 15387ED314949D2A

FASTA40844,791
        10         20         30         40         50         60 
MANINENYLK LKAGYLFPEI SKRVKIYSEK NPSAKIIRLG IGDVTLPIVP SVVDAMVEAS 

        70         80         90        100        110        120 
KEMGTVGGFH GYGPEQGYSF LLKSIADHDY GSLGIKIDES EIFVSDGSKC DCGNIQEIFS 

       130        140        150        160        170        180 
TDSKIAVADP VYPVYVDTNV MAGRTGEIGP DGRYSNLIYM PATKENGFQP EIPKEKADIV 

       190        200        210        220        230        240 
YLCYPNNPTG TVTTKESLKA WVEYAKKNNS IILYDSAYEA FISEPGVPRS IYEVEGAKEV 

       250        260        270        280        290        300 
AIEFRSFSKT AGFTGLRCAY IVIPKELKGK TRSGEEVSLN SLWNRRHTTK FNGVSYVTQK 

       310        320        330        340        350        360 
GAEACYSPQG KKEIQTSIAY YMANASKIRD GLKKAGYEVF GGVNAPYIWL KTSDNLSSWD 

       370        380        390        400 
FFDKLLNKAQ VVGTPGSGFG PAGEGYFRLS AFGKKEDVEE AIARITSL 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN47975.1.
RefSeqNP_710957.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F814.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA0776.

Proteomic databases

PaxDbQ8F814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN47975; AAN47975; LA_0776.
GeneID1150119.
KEGGlil:LA_0776.
PATRIC22382410. VBILepInt91350_0782.

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
OMASAYAMYI.
OrthoDBEOG6XWV2X.
ProtClustDBPRK07590.

Enzyme and pathway databases

BioCycLINT189518:GJBB-629-MONOMER.
UniPathwayUPA00034; UER00466.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01642. DapL_aminotrans_1.
InterProIPR004839. Aminotransferase_I/II.
IPR019942. DapL_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11751:SF22. PTHR11751:SF22. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR03542. DAPAT_plant. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDAPAT_LEPIN
AccessionPrimary (citable) accession number: Q8F814
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 71 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