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Q31PY6 (DAPAT_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 53. 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:Synpcc7942_0853
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus ›

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_0000312550

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
Q31PY6 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 3BCDA337CE482057

FASTA41144,846
        10         20         30         40         50         60 
MATINDNYLK LKAGYLFPEI ARRVNAFAQS NPEAAIIRLG IGDVTEPLPV ACRQAMIQAV 

        70         80         90        100        110        120 
EDMGQRENFK GYGPEQGYAW LREKIAAHDF QSRGCEVDAS EIFISDGSKC DCGNILDIFG 

       130        140        150        160        170        180 
NNNRIAVTDP VYPVYVDTNV MAGHTGDAND RGEYDGLVYL PISAENNFTA EIPSEKVDLI 

       190        200        210        220        230        240 
YLCFPNNPTG AVASREYLQA WVDYARANGA IILFDAAYEA FITDPAIPHS IFEIPGARDC 

       250        260        270        280        290        300 
AIEFRSFSKN AGFTGTRCAF TVVPKGLKGK AADGSEVELW GLWNRRQSTK FNGVSYIVQR 

       310        320        330        340        350        360 
GAEAVYSAEG QAQIKELVAF YLENARIIRE ELTAAGLDVH GGVNAPYVWV KTPAGLTSWD 

       370        380        390        400        410 
FFDKLLQVCN VVGTPGSGFG AAGEGYFRIS AFNSRENVVT AMQRIRSAGL A

« Hide

References

[1]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000100 Genomic DNA. Translation: ABB56883.1.
RefSeqYP_399870.1. NC_007604.1.

3D structure databases

ProteinModelPortalQ31PY6.
ModBaseSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_0853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB56883; ABB56883; Synpcc7942_0853.
GeneID3774029.
KEGGsyf:Synpcc7942_0853.
PATRIC23786923. VBISynElo51371_0995.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
ProtClustDBPRK07590.

Enzyme and pathway databases

BioCycSELO1140:GJWQ-869-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_SYNE7
AccessionPrimary (citable) accession number: Q31PY6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 53 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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