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Q30ZX9 (DAPAT_DESDG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Dde_1970
OrganismDesulfovibrio desulfuricans (strain G20) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio ›

Protein attributes

Sequence length388 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.

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.

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 – 388388LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_0000342235

Sites

Binding site411Substrate; via amide nitrogen By similarity
Binding site671Pyridoxal phosphate; shared with dimeric partner By similarity
Binding site1291Substrate By similarity
Binding site1791Pyridoxal phosphate By similarity
Binding site1791Substrate By similarity
Binding site2071Pyridoxal phosphate By similarity
Binding site2101Pyridoxal phosphate By similarity
Binding site2391Pyridoxal phosphate By similarity
Binding site2411Pyridoxal phosphate By similarity
Binding site2501Pyridoxal phosphate By similarity
Binding site3681Substrate By similarity

Amino acid modifications

Modified residue2421N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30ZX9 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 68CA2F7BA4A6942C

FASTA38842,773
        10         20         30         40         50         60 
MTQFTLADRL ATLPPYLFAQ IDKVKAEVAA RGVDIISLGI GDPDMPTPDF VIEALKKAAE 

        70         80         90        100        110        120 
KPANHQYPSY TGMLAFRQEV ANWYKRRYAV ELDPKTEVLT LIGSKEGIAH FPTAFVNPGD 

       130        140        150        160        170        180 
LVLVCPPCYP VYAIASRFMG GVVQELPLLE ENDFLPDLDA VDEATWEKAR CIFVNYPNNP 

       190        200        210        220        230        240 
TAAMAPRSFF EKLIGIARKH NVIVVHDAAY TEMYYNENNR PLSIMEIPGA MDVAIEFNSL 

       250        260        270        280        290        300 
SKPYNMTGWR IAMAVGNASL VAGLGKVKEN MDSGAFQAVQ EAAIVALRDG DAFLAEIRDI 

       310        320        330        340        350        360 
YRKRRDTVIA ALNKIGITCR VPEASLYVWA RVPEGYTSSD FVTRVLQETG VVMTPGNGFG 

       370        380 
AAGEGYFRIS LTVNDERLEE AVSRIASL

« Hide

References

[1]"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20."
Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. expand/collapse author list , Lapidus A.L., Palumbo A.V., Wall J.D.
J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000112 Genomic DNA. Translation: ABB38767.1.
RefSeqYP_388462.1. NC_007519.1.

3D structure databases

ProteinModelPortalQ30ZX9.
ModBaseSearch...

Protein-protein interaction databases

STRING207559.Dde_1970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB38767; ABB38767; Dde_1970.
GeneID3756976.
KEGGdde:Dde_1970.
PATRIC21742873. VBIDesDes50040_1949.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223051.
KOK10206.
OMAWRIAMAV.
ProtClustDBPRK09276.

Enzyme and pathway databases

BioCycDALA207559:GH1L-1750-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.
IPR019881. DAP-NH2Trfase_DapL_Desulfo.
IPR019942. DAP_NH2Trfase_plant/Chlamydia.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR03540. DapC_direct. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPAT_DESDG
AccessionPrimary (citable) accession number: Q30ZX9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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