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C4ZG66 (DAPAT_EUBR3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:EUBREC_2541
OrganismEubacterium rectale (strain ATCC 33656 / VPI 0990) [Complete proteome] [HAMAP]
Taxonomic identifier515619 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length404 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 – 404404LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_1000215831

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 site1881Pyridoxal phosphate By similarity
Binding site1881Substrate By similarity
Binding site2161Pyridoxal phosphate By similarity
Binding site2191Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site2491Pyridoxal phosphate By similarity
Binding site2581Pyridoxal phosphate By similarity
Binding site2881Substrate; shared with dimeric partner By similarity
Binding site3841Substrate By similarity

Amino acid modifications

Modified residue2501N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C4ZG66 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 5D68F2871E0BB880

FASTA40444,267
        10         20         30         40         50         60 
MFQINDNFQK LPGSYLFSTI AKKVAAYQEA NPDKEIIRLG IGDVTQPLAP AIIDALHKAV 

        70         80         90        100        110        120 
DEMGNAATFH GYAPDLGYEF LRKAISDNDY KARGCDISAD EIFVSDGAKS DSANIQELFS 

       130        140        150        160        170        180 
ANSRIAVTDP VYPVYVDSNV MAGRTGTYDA QTETWSNVIY MPSTADNGFV PELPKEVPDM 

       190        200        210        220        230        240 
IYLCLPNNPT GTTLKKEQLQ VWVDYANKNG SVIIFDAAYE AYISEADVPH SIYECNGAKT 

       250        260        270        280        290        300 
CAIELRSFSK NAGFTGVRLG FTVVPKELKC GDVSLHAMWA RRHGTKFNGA PYIVQRAGEA 

       310        320        330        340        350        360 
VYSDAGKAQL KDQVAYYMNN AKTIKTGLAE AGFTVYGGVN APYIWLKTPD QMTSWEFFDY 

       370        380        390        400 
LLENANVVGT PGSGFGPSGE GYFRLTAFGN YENTVKALER IKAL 

« Hide

References

[1]"Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla."
Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., Hettich R.L., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33656 / VPI 0990.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001107 Genomic DNA. Translation: ACR76272.1.
RefSeqYP_002938406.1. NC_012781.1.

3D structure databases

ProteinModelPortalC4ZG66.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING515619.EUBREC_2541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR76272; ACR76272; EUBREC_2541.
GeneID7966566.
KEGGere:EUBREC_2541.
PATRIC21873135. VBIEubRec107985_2207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
OMAKWVDYAN.
OrthoDBEOG6XWV2X.

Enzyme and pathway databases

BioCycEREC515619:GHMX-2530-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_EUBR3
AccessionPrimary (citable) accession number: C4ZG66
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 35 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