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O84395 (DAPAT_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:aspC
Ordered Locus Names:CT_390
OrganismChlamydia trachomatis
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Is also able to use meso-diaminopimelate, cystathionine, lysine or ornithine as substrates. Ref.1

Catalytic activity

LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O. Ref.1

Cofactor

Pyridoxal phosphate. Ref.1

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1. HAMAP MF_01642

Subunit structure

Homodimer By similarity. HAMAP MF_01642

Developmental stage

Expressed as early as 8 hours after infection. Ref.1

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=116 µM for LL-2,6-diaminopimelate (at 30 degrees Celsius and pH 7.6) Ref.1

KM=2.1 mM for 2-oxoglutarate (at 30 degrees Celsius and pH 7.6)

KM=19 µM for L-2,3,4,5-tetrahydrodipicolinate (at 30 degrees Celsius and pH 7.6)

KM=4.0 mM for glutamic acid (at 30 degrees Celsius and pH 7.6)

Vmax=0.58 µmol/min/mg enzyme for the forward reaction (at 30 degrees Celsius and pH 7.6)

Vmax=0.01 µmol/min/mg enzyme for the reverse reaction (at 30 degrees Celsius and pH 7.6)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394LL-diaminopimelate aminotransferase HAMAP MF_01642
PRO_0000312004

Sites

Binding site411Substrate; via amide nitrogen By similarity
Binding site711Pyridoxal phosphate; shared with dimeric partner By similarity
Binding site741Substrate; shared with dimeric partner By similarity
Binding site1051Substrate By similarity
Binding site1281Substrate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site1741Substrate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2051Pyridoxal phosphate By similarity
Binding site2331Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2441Pyridoxal phosphate By similarity
Binding site2751Substrate; shared with dimeric partner By similarity
Binding site3691Substrate By similarity

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict921F → C in ABN58777. Ref.1
Sequence conflict1061V → A in ABN58777. Ref.1

Secondary structure

1 ..................................................................... 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O84395 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 98437E24E6D55AAE

FASTA39443,841
        10         20         30         40         50         60 
MKRNPHFVSL TKNYLFADLQ KRVAQFRLEN PQHTVINLSI GDTTQPLNAS VAEAFASSIA 

        70         80         90        100        110        120 
RLSSPTTCRG YGPDFGLPAL RQKLSEDFYR GFVDAKEIFI SDGAKVDLFR LLSFFGPNQT 

       130        140        150        160        170        180 
VAIQDPSYPA YLDIARLTGA KEIIALPCLQ ENAFFPEFPE DTHIDILCLC SPNNPTGTVL 

       190        200        210        220        230        240 
NKDQLRAIVH YAIEHEILIL FDAAYSTFIS DPSLPKSIFE IPDARFCAIE INSFSKPLGF 

       250        260        270        280        290        300 
AGIRLGWTVI PQELTYADGH FVIQDWERFL STTFNGASIP AQEAGVAGLS ILPQLEAIHY 

       310        320        330        340        350        360 
YRENSDLLRK ALLATGFEVF GGEHAPYLWV KPTQANISDR DLFDFFLREY HIAITPGIGF 

       370        380        390 
GRSGSGFVRF SSLGKREDIL AACERLQMAP ALQS

« Hide

References

« Hide 'large scale' references
[1]"L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine."
McCoy A.J., Adams N.E., Hudson A.O., Gilvarg C., Leustek T., Maurelli A.T.
Proc. Natl. Acad. Sci. U.S.A. 103:17909-17914(2006) [PubMed: 17093042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DEVELOPMENTAL STAGE, SUBSTRATE SPECIFICITY.
Strain: L2.
[2]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EF396248 Genomic DNA. Translation: ABN58777.1.
AE001273 Genomic DNA. Translation: AAC67987.2.
PIRD71520.
RefSeqNP_219900.1. NC_000117.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ASAX-ray2.05A1-394[»]
3ASBX-ray2.70A1-394[»]
ProteinModelPortalO84395.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID884727.
GenomeReviewsGene locus CT_390 in contig AE001273_GR.
KEGGctr:CT390.
PATRIC20380331. VBIChlTra43535_0420.

Phylogenomic databases

HOGENOMHBG645860.
OMAENTHIDI.
ProtClustDBPRK07590.

Family and domain databases

HAMAPMF_01642. DapL_aminotrans_1.
[Tree]
InterProIPR004839. Aminotransferase_I/II.
IPR019942. DAP_NH2Trfase_plant/Chlamydia.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK10206.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPAT_CHLTR
AccessionPrimary (citable) accession number: O84395
Secondary accession number(s): A3FKT7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 70 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents