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Q1MR87 (DAPAT_LAWIP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:LI0435
OrganismLawsonia intracellularis (strain PHE/MN1-00) [Complete proteome] [HAMAP]
Taxonomic identifier363253 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeLawsonia

Protein attributes

Sequence length410 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 – 410410LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_0000342243

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 site1861Pyridoxal phosphate By similarity
Binding site1861Substrate By similarity
Binding site2141Pyridoxal phosphate By similarity
Binding site2171Pyridoxal phosphate By similarity
Binding site2451Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site2561Pyridoxal phosphate By similarity
Binding site2911Substrate; shared with dimeric partner By similarity
Binding site3871Substrate By similarity

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MR87 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: C6E829F1020272F2

FASTA41045,941
        10         20         30         40         50         60 
MAHTNKHYLD LPGSYFFTEI NQRVNTYKKT HPEKSIIRLS IGDVTRPLVP AVIKALHDAT 

        70         80         90        100        110        120 
DEMGQPSSFH GYGPEHGYEF LIGEIIANDY TSRNVHIEAD EIFVSDGTKC DIANIQELFD 

       130        140        150        160        170        180 
PSDTVAIIDP VYPVYIDSNV MSGRLGKLIN GIWSKLIYLP CTIENNFIPE LPTQHPDIIY 

       190        200        210        220        230        240 
LCYPNNPTGT VLSKDQLTIW VNYAKKEGAI ILFDAAYEAY ITDPTIPHSI YEIDGAKEVA 

       250        260        270        280        290        300 
IEFRSFSKTA GFTGLRCAYT VIPKELKANT REGNEQYLNM MWNRRQTTKY NGCSYIVQKA 

       310        320        330        340        350        360 
AAAIYTPEGQ KQIQESIQYY MKNALIIQNA ITQMGITAVG GINAPYVWIK TPDNLSSWDF 

       370        380        390        400        410 
FDLLLQNAGV VGTPGVGFGP HGEGYFRLTG FGSYEDTNKA IERIQKALLI 

« Hide

References

[1]"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHE/MN1-00.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180252 Genomic DNA. Translation: CAJ54489.1.
RefSeqYP_594811.1. NC_008011.1.

3D structure databases

ProteinModelPortalQ1MR87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING363253.LI0435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4059387.
KEGGlip:LI0435.
PATRIC22304279. VBILawInt40445_0479.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
OMAKCAIEFR.
OrthoDBEOG6XWV2X.
ProtClustDBPRK07590.

Enzyme and pathway databases

BioCycLINT363253:GH6E-449-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_LAWIP
AccessionPrimary (citable) accession number: Q1MR87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 58 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