Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P95468

- TYRB_PARDE

UniProt

P95468 - TYRB_PARDE

Protein

Aromatic-amino-acid aminotransferase

Gene

tyrB

Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

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

    GO - Biological processi

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

    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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394Aromatic-amino-acid aminotransferasePRO_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

    1
    394
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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...
    MobiDBi 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: October 1, 2014
    This is version 87 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