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B1WSG7 (DAPAT_CYAA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:cce_2605
OrganismCyanothece sp. (strain ATCC 51142) [Complete proteome] [HAMAP]
Taxonomic identifier43989 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length411 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 – 411411LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_1000186860

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
B1WSG7 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 97CAC8BC8F6A582C

FASTA41145,374
        10         20         30         40         50         60 
MATINDNYLK LKAGYLFPEI ARRVNTFIEA NPEAKIIKLG IGDVTEPLPE ACRTAMIKAV 

        70         80         90        100        110        120 
EDMGDRSSFK GYGPEQGYGW LREKIAAQDF QARGCDIDAS EIFVSDGAKC DTGNILDIFG 

       130        140        150        160        170        180 
KNNKIAVTDP VYPVYVDTNV MAGHTGETNE KGEYEGLVYL PISADNHFVA DIPSEKVDLI 

       190        200        210        220        230        240 
YLCFPNNPTG ATATKEYLKA WVDYATANDS IIFFDAAYEA FITDESLPHS IYEIEGAKDC 

       250        260        270        280        290        300 
AIEFRSFSKN AGFTGTRCAF TVVPKQLTAK ASDGSQVELW KLWNRRQSTK FNGVSYIVQR 

       310        320        330        340        350        360 
GAEAVYSEAG KAQIKGLVSF YLENAKIICE QLKSAGFEVY GGVNAPYIWL KTPHNLSSWD 

       370        380        390        400        410 
FFDKLLQTTH VVGTPGSGFG AAGEGYFRIS AFNSRENVEE AMKRITQAFK V 

« Hide

References

[1]"The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium important in the marine nitrogen cycle."
Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.
Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51142.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000806 Genomic DNA. Translation: ACB51953.1.
RefSeqYP_001804019.1. NC_010546.1.

3D structure databases

ProteinModelPortalB1WSG7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING43989.cce_2605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB51953; ACB51953; cce_2605.
GeneID6169662.
KEGGcyt:cce_2605.
PATRIC21543636. VBICyaSp130209_2639.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCSP43989:GKC8-2641-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_CYAA5
AccessionPrimary (citable) accession number: B1WSG7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 43 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