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B7KL61 (DAPAT_CYAP7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 33. 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:PCC7424_4059
OrganismCyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155)) [Complete proteome] [HAMAP]
Taxonomic identifier65393 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Cyanothece

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.

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 – 411411LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_1000186862

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
B7KL61 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 82058D26638A9434

FASTA41145,272
        10         20         30         40         50         60 
MATINDNYLK LKAGYLFPEI ARRVNAFAEA HPEAKIIKLG IGDVTEPLPQ ACRQAMIKAV 

        70         80         90        100        110        120 
EEMGDRATFK GYGPEQGYNW LREKIAQNDF QARGCDIDAS EIFISDGSKC DTGNILDIFG 

       130        140        150        160        170        180 
KNNTIAVTDP VYPVYVDTNV MAGHTGDAND KGEYLGLVYL PMTANNNFTP ELPSQKVDLI 

       190        200        210        220        230        240 
YLCFPNNPTG ATATKENLTK WVNYAKENGS IIFFDAAYEA FITDPSLPHS IYEIEGARDC 

       250        260        270        280        290        300 
AIEFRSFSKN AGFTGTRCAL TVVPKTLKAK ASDGSEVELW KLWNRRQSTK FNGVSYIVQR 

       310        320        330        340        350        360 
GAEAVYSEEG QAQVKALVNF YLENAKIICD KLSFAGLTVY GGVNAPYVWV KTPDGLSSWD 

       370        380        390        400        410 
FFDKLLQSAN VVGTPGSGFG AAGEGYFRIS AFNSRENVEE ATRRIIEKLT V

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001291 Genomic DNA. Translation: ACK72433.1.
RefSeqYP_002379301.1. NC_011729.1.

3D structure databases

ProteinModelPortalB7KL61.
ModBaseSearch...

Protein-protein interaction databases

STRING65393.PCC7424_4059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK72433; ACK72433; PCC7424_4059.
GeneID7108977.
KEGGcyc:PCC7424_4059.
PATRIC21557116. VBICyaSp136448_4157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
OMAQDFQARG.
ProtClustDBPRK07590.

Enzyme and pathway databases

BioCycCSP65393:GJP7-4106-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. DAP_NH2Trfase_plant/Chlamydia.
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. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR03542. DAPAT_plant. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPAT_CYAP7
AccessionPrimary (citable) accession number: B7KL61
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 33 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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