Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3AMU5 (DAPAT_SYNSC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:Syncc9605_0311
OrganismSynechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]
Taxonomic identifier110662 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length408 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 – 408408LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_0000312546

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
Q3AMU5 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 0D71757E6B2AC677

FASTA40844,036
        10         20         30         40         50         60 
MVQVNGNYLK LKAGYLFPEI GRRVKAFSSA NPDAALIRLG IGDVTEPLPL ACREAMKTAI 

        70         80         90        100        110        120 
DAMGTAEGFH GYGPEQGYGW LREAIAKNDF QARGCDISAE EIFVSDGSKC DSSNILDILG 

       130        140        150        160        170        180 
EGNKVAVTDP VYPVYVDSNV MAGRTGEAGE IGRYAGLTYL PISADNGFAA LIPSEPVDLI 

       190        200        210        220        230        240 
YLCFPNNPTG AVATREQLQA WVNYARANGA LILFDAAYEA FIQDPELPRS IFEIEGARDC 

       250        260        270        280        290        300 
AIEFRSFSKN AGFTGTRCAF TVVPKGLKGK AANGEAVELW GLWNRRQSTK FNGVSYIIQR 

       310        320        330        340        350        360 
GAEAVYSEAG QAEVKALVSF YMENAAIIRR ELTAAGLTVY GGEHAPYVWI KTPEGMDSWG 

       370        380        390        400 
FFDHLLNKAN VVGTPGSGFG AAGECYFRLS AFNSRANVDE AMARIKAL 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9605."
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., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9605.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000110 Genomic DNA. Translation: ABB34087.1.
RefSeqYP_380642.1. NC_007516.1.

3D structure databases

ProteinModelPortalQ3AMU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING110662.Syncc9605_0311.

Proteomic databases

PRIDEQ3AMU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB34087; ABB34087; Syncc9605_0311.
GeneID3737545.
KEGGsyd:Syncc9605_0311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
OMAKCAIEFR.
OrthoDBEOG6XWV2X.
ProtClustDBPRK07590.

Enzyme and pathway databases

BioCycSSP110662:GJ7R-319-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_SYNSC
AccessionPrimary (citable) accession number: Q3AMU5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 66 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