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Q8YP73 (DAPT2_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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 2

Short name=DAP-AT 2
Short name=DAP-aminotransferase 2
Short name=LL-DAP-aminotransferase 2
EC=2.6.1.83
Gene names
Name:dapL2
Ordered Locus Names:all4327
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length390 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 – 390390LL-diaminopimelate aminotransferase 2 HAMAP-Rule MF_01642
PRO_0000342210

Sites

Binding site381Substrate; via amide nitrogen By similarity
Binding site641Pyridoxal phosphate; shared with dimeric partner By similarity
Binding site1271Substrate By similarity
Binding site1771Pyridoxal phosphate By similarity
Binding site1771Substrate By similarity
Binding site2051Pyridoxal phosphate By similarity
Binding site2081Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site3651Substrate By similarity

Amino acid modifications

Modified residue2391N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YP73 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 6CFB39A6C8C32E8F

FASTA39043,225
        10         20         30         40         50         60 
MQFAKRLEKI PPYLFAEINR KREALIAKGV DIINIGVGDP DKPTPAHILQ AMREAIDDAS 

        70         80         90        100        110        120 
NHNYPPYEGT QEFREAAVEW MERRFGVMDL NPNTEVVSSI GSKEAIHNTF LAFVEAGDYT 

       130        140        150        160        170        180 
LIPDPGYPVY RTSTIFAGGE AFSMPLKAEN KFLPDLDLIP EEVARKAKML WINYPNNPTG 

       190        200        210        220        230        240 
ALATLEFFEE LVALCQQYSI LLCHDHAYSE MAYDGYKPPS VLQIPGAKDI AIEFHSLSKS 

       250        260        270        280        290        300 
YNMTGWRIGF AVGNAYAIKG LSQVKTNVDS GVFKAIQKAA IAAYATDEVE LQAVMSVYQS 

       310        320        330        340        350        360 
RRDIIVKGLQ SLGWPIEPPK ATLYVWVPVP PGYTSTEFTT LLLDKCGIVV PPGVGYGASG 

       370        380        390 
EGYFRVALTI SDERLHEAIQ RMQDAGIRYA 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB76026.1.
PIRAH2346.
RefSeqNP_488367.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YP73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING103690.all4327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB76026; BAB76026; BAB76026.
GeneID1107929.
KEGGana:all4327.
PATRIC22779226. VBINosSp37423_5060.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223051.
KOK10206.
OMAFYIWAPV.
OrthoDBEOG6W721W.
ProtClustDBPRK09276.

Enzyme and pathway databases

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.
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. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPT2_NOSS1
AccessionPrimary (citable) accession number: Q8YP73
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 77 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