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Q9Z856 (DAPAT_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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:CPn_0495, CP_0259, CPj0495, CpB0515
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length397 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 caution

The sequence AAP98444.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397LL-diaminopimelate aminotransferase HAMAP-Rule MF_01642
PRO_0000342219

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 site3681Substrate By similarity

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z856 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 42D7A6C97983D137

FASTA39744,491
        10         20         30         40         50         60 
MRRNPHFSLL KPQYLFSEIS KKLAQFRKEN PEISVIDLSI GDTTQPLCRS ITQAIKEFCV 

        70         80         90        100        110        120 
SQEKQETYRG YGPETGLEKL RTKIASEVYE NRISPEEIFI SDGAKPDIFR LFSFFGSEKT 

       130        140        150        160        170        180 
LGLQDPVYPA YRDIAHITGI RDIIPLACRK ETGFIPELPN QQSLDILCLC YPNNPTGTVL 

       190        200        210        220        230        240 
TFQQLQALVN YANQHGTVLI FDAAYSAFVS DPSLPKSIFE IPEAKYCAIE INSFSKSLGF 

       250        260        270        280        290        300 
TGMRLAWNVI PKELTYDNNE PMINDWKRLF ATTFNGASLL MQEAGYYGLD LFPTPPAISL 

       310        320        330        340        350        360 
YLTNAQKLKK SLETAGFSVH GGDHAPYLWV ELPEGISDEE AFDFFLHQYH IAVTPGHGFG 

       370        380        390 
SCGQGFVRFS ALTQPQNIAL ACDRLCTASL KETMVLA 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD18635.1.
AE002161 Genomic DNA. Translation: AAF73649.1.
BA000008 Genomic DNA. Translation: BAA98701.1.
AE009440 Genomic DNA. Translation: AAP98444.1. Different initiation.
PIRC86552.
F72072.
RefSeqNP_224691.1. NC_000922.1.
NP_300550.1. NC_002491.1.
NP_444810.1. NC_002179.2.
NP_876787.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z856.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD18635; AAD18635; CPn_0495.
AAF73649; AAF73649; CP_0259.
AAP98444; AAP98444; CpB0515.
BAA98701; BAA98701; BAA98701.
GeneID1467194.
895445.
919237.
962904.
KEGGcpa:CP0259.
cpj:CPj0495.
cpn:CPn0495.
cpt:CpB0515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223061.
KOK10206.
OMAKWVDYAN.
OrthoDBEOG6XWV2X.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-272-MONOMER.
CPNE115713:GHEY-511-MONOMER.
CPNE138677:GH8N-504-MONOMER.
CPNE182082:GH4N-525-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.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
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.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPAT_CHLPN
AccessionPrimary (citable) accession number: Q9Z856
Secondary accession number(s): Q7AIP4, Q7DEX0, Q7VPZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 98 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