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P95468 (TYRB_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. 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:
Aromatic-amino-acid aminotransferase

Short name=ARAT
Short name=AROAT
EC=2.6.1.57
Gene names
Name:tyrB
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

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

General annotation (Comments)

Function

Shows activities toward both dicarboxylic and aromatic substrates.

Catalytic activity

An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Aromatic-amino-acid aminotransferase
PRO_0000123894

Sites

Binding site341Substrate; via amide nitrogen
Binding site651Substrate
Binding site1271Substrate
Binding site1801Substrate
Binding site3711Substrate

Amino acid modifications

Modified residue2431N6-(pyridoxal phosphate)lysine

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P95468 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 092FC4643F1E387A

FASTA39442,732
        10         20         30         40         50         60 
MLGNLKPQAP DKILALMGEF RADPRQGKID LGVGVYKDAT GHTPIMRAVH AAEQRMLETE 

        70         80         90        100        110        120 
TTKTYAGLSG EPEFQKAMGE LILGDGLKSE TTATLATVGG TGALRQALEL ARMANPDLRV 

       130        140        150        160        170        180 
FVSDPTWPNH VSIMNFMGLP VQTYRYFDAE TRGVDFEGMK ADLAAAKKGD MVLLHGCCHN 

       190        200        210        220        230        240 
PTGANLTLDQ WAEIASILEK TGALPLIDLA YQGFGDGLEE DAAGTRLIAS RIPEVLIAAS 

       250        260        270        280        290        300 
CSKNFGIYRE RTGCLLALCA DAATRELAQG AMAFLNRQTY SFPPFHGAKI VSTVLTTPEL 

       310        320        330        340        350        360 
RADWMAELEA VRSGMLRLRE QLAGELRDLS GSDRFGFVAE HRGMFSRLGA TPEQVKRIKE 

       370        380        390 
EFGIYMVGDS RINIAGLNDN TIPILARAII EVGV 

« Hide

References

[1]"Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism."
Oue S., Okamoto A., Nakai Y., Nakahira M., Shibatani T., Hayashi H., Kagamiyama H.
J. Biochem. 121:161-171(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NBRC 12442.
[2]"Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network."
Okamoto A., Nakai Y., Hayashi H., Hirotsu K., Kagamiyama H.
J. Mol. Biol. 280:443-461(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND SUBSTRATE ANALOGS, SUBUNIT.
[3]"The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity."
Okamoto A., Ishii S., Hirotsu K., Kagamiyama H.
Biochemistry 38:1176-1184(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND SUBSTRATE ANALOGS, PYRIDOXAL PHOSPHATE AT LYS-243.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08272 Genomic DNA. Translation: CAA69597.1.
PIRJC5197.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AY4X-ray2.33A/B1-394[»]
1AY5X-ray2.50A/B1-394[»]
1AY8X-ray2.30A/B1-394[»]
2AY1X-ray2.20A/B1-394[»]
2AY2X-ray2.40A/B1-394[»]
2AY3X-ray2.40A/B1-394[»]
2AY4X-ray2.20A/B1-394[»]
2AY5X-ray2.40A/B1-394[»]
2AY6X-ray2.20A/B1-394[»]
2AY7X-ray2.40A/B1-394[»]
2AY8X-ray2.20A/B1-394[»]
2AY9X-ray2.50A/B1-394[»]
ProteinModelPortalP95468.
SMRP95468. Positions 1-394.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.6.1.57. 4529.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP95468.

Entry information

Entry nameTYRB_PARDE
AccessionPrimary (citable) accession number: P95468
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references