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P95468

- TYRB_PARDE

UniProt

P95468 - TYRB_PARDE

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Protein
Aromatic-amino-acid aminotransferase
Gene
tyrB
Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Shows activities toward both dicarboxylic and aromatic substrates.

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341Substrate; via amide nitrogen
Binding sitei65 – 651Substrate
Binding sitei127 – 1271Substrate
Binding sitei180 – 1801Substrate
Binding sitei371 – 3711Substrate

GO - Molecular functioni

  1. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  2. aromatic-amino-acid:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  3. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.57. 4529.

Names & Taxonomyi

Protein namesi
Recommended name:
Aromatic-amino-acid aminotransferase (EC:2.6.1.57)
Short name:
ARAT
Short name:
AROAT
Gene namesi
Name:tyrB
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Aromatic-amino-acid aminotransferase
PRO_0000123894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei243 – 2431N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43
Helixi13 – 2210
Helixi47 – 5913
Helixi72 – 8312
Helixi84 – 863
Helixi89 – 913
Beta strandi92 – 987
Helixi99 – 11416
Beta strandi120 – 1256
Helixi128 – 13710
Beta strandi141 – 1455
Turni149 – 1524
Helixi156 – 1649
Beta strandi171 – 1788
Turni180 – 1823
Helixi188 – 20114
Beta strandi204 – 2096
Beta strandi214 – 2163
Helixi218 – 23114
Beta strandi233 – 2408
Turni242 – 2465
Helixi248 – 2503
Beta strandi252 – 2587
Helixi262 – 27716
Beta strandi280 – 2823
Helixi286 – 29611
Helixi298 – 33033
Beta strandi331 – 3333
Turni334 – 3363
Helixi337 – 3404
Beta strandi343 – 3475
Helixi352 – 36211
Beta strandi371 – 3733
Helixi374 – 3763
Turni379 – 3813
Helixi382 – 39211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP95468.
SMRiP95468. Positions 1-394.

Miscellaneous databases

EvolutionaryTraceiP95468.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

P95468-1 [UniParc]FASTAAdd to Basket

« Hide

MLGNLKPQAP DKILALMGEF RADPRQGKID LGVGVYKDAT GHTPIMRAVH    50
AAEQRMLETE TTKTYAGLSG EPEFQKAMGE LILGDGLKSE TTATLATVGG 100
TGALRQALEL ARMANPDLRV FVSDPTWPNH VSIMNFMGLP VQTYRYFDAE 150
TRGVDFEGMK ADLAAAKKGD MVLLHGCCHN PTGANLTLDQ WAEIASILEK 200
TGALPLIDLA YQGFGDGLEE DAAGTRLIAS RIPEVLIAAS CSKNFGIYRE 250
RTGCLLALCA DAATRELAQG AMAFLNRQTY SFPPFHGAKI VSTVLTTPEL 300
RADWMAELEA VRSGMLRLRE QLAGELRDLS GSDRFGFVAE HRGMFSRLGA 350
TPEQVKRIKE EFGIYMVGDS RINIAGLNDN TIPILARAII EVGV 394
Length:394
Mass (Da):42,732
Last modified:May 1, 1997 - v1
Checksum:i092FC4643F1E387A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08272 Genomic DNA. Translation: CAA69597.1.
PIRiJC5197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08272 Genomic DNA. Translation: CAA69597.1 .
PIRi JC5197.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AY4 X-ray 2.33 A/B 1-394 [» ]
1AY5 X-ray 2.50 A/B 1-394 [» ]
1AY8 X-ray 2.30 A/B 1-394 [» ]
2AY1 X-ray 2.20 A/B 1-394 [» ]
2AY2 X-ray 2.40 A/B 1-394 [» ]
2AY3 X-ray 2.40 A/B 1-394 [» ]
2AY4 X-ray 2.20 A/B 1-394 [» ]
2AY5 X-ray 2.40 A/B 1-394 [» ]
2AY6 X-ray 2.20 A/B 1-394 [» ]
2AY7 X-ray 2.40 A/B 1-394 [» ]
2AY8 X-ray 2.20 A/B 1-394 [» ]
2AY9 X-ray 2.50 A/B 1-394 [» ]
ProteinModelPortali P95468.
SMRi P95468. Positions 1-394.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 2.6.1.57. 4529.

Miscellaneous databases

EvolutionaryTracei P95468.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11879. PTHR11879. 1 hit.
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
PRINTSi PR00799. TRANSAMINASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTYRB_PARDE
AccessioniPrimary (citable) accession number: P95468
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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