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Protein

Tyrosine ammonia-lyase

Gene

hutH

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the non-oxidative deamination of L-tyrosine. Has very low phenylalanine ammonia-lyase activity (in vitro).1 Publication

Catalytic activityi

L-tyrosine = trans-p-hydroxycinnamate + ammonia.1 Publication

Kineticsi

kcat is 4.32 sec(-1) for L-Tyr. kcat is 13.1 sec(-1) for L-Phe.

  1. KM=74.2 µM for L-Tyr1 Publication
  2. KM=11400 µM for L-Phe1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei60 – 601Proton donor/acceptorBy similarity
    Binding sitei89 – 891Substrate
    Binding sitei303 – 3031Substrate

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • tyrosine ammonia-lyase activity Source: UniProtKB

    GO - Biological processi

    • phenylpropanoid biosynthetic process Source: UniProtKB
    • protein homotetramerization Source: UniProtKB
    • tyrosine catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Phenylpropanoid metabolism

    Enzyme and pathway databases

    BioCyciRSPH272943:GJAS-3700-MONOMER.
    SABIO-RKQ3IWB0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine ammonia-lyase (EC:4.3.1.23)
    Gene namesi
    Name:hutH
    ORF Names:RSP_3574
    OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
    Taxonomic identifieri272943 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
    Proteomesi
    • UP000002703 Componenti: Chromosome 2

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891H → F: Abolishes tyrosine ammonia-lyase activity. Increases affinity for L-Phe. Increases the low intrinsic phenylalanine ammonia-lyase activity about twentyfold.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 523523Tyrosine ammonia-lyasePRO_0000429968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki149 ↔ 1515-imidazolinone (Ala-Gly)
    Modified residuei150 – 15012,3-didehydroalanine (Ser)

    Post-translational modificationi

    Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-9544445,EBI-9544445

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    STRINGi272943.RSP_3574.

    Structurei

    Secondary structure

    1
    523
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 156Combined sources
    Helixi19 – 268Combined sources
    Beta strandi29 – 346Combined sources
    Helixi36 – 5419Combined sources
    Turni60 – 623Combined sources
    Helixi67 – 715Combined sources
    Helixi76 – 783Combined sources
    Helixi79 – 9012Combined sources
    Beta strandi94 – 974Combined sources
    Helixi100 – 11415Combined sources
    Helixi123 – 13311Combined sources
    Beta strandi142 – 1443Combined sources
    Beta strandi148 – 1514Combined sources
    Helixi153 – 16311Combined sources
    Helixi179 – 1857Combined sources
    Helixi198 – 2003Combined sources
    Beta strandi203 – 2053Combined sources
    Helixi206 – 23631Combined sources
    Helixi241 – 2444Combined sources
    Helixi246 – 2516Combined sources
    Helixi255 – 26713Combined sources
    Turni268 – 2703Combined sources
    Beta strandi272 – 2754Combined sources
    Helixi279 – 2813Combined sources
    Helixi286 – 2883Combined sources
    Helixi300 – 3034Combined sources
    Helixi305 – 32723Combined sources
    Beta strandi333 – 3353Combined sources
    Beta strandi341 – 3433Combined sources
    Helixi353 – 38028Combined sources
    Turni383 – 3886Combined sources
    Helixi391 – 3933Combined sources
    Beta strandi396 – 3983Combined sources
    Helixi405 – 41915Combined sources
    Helixi425 – 4273Combined sources
    Turni432 – 4354Combined sources
    Helixi442 – 47534Combined sources
    Turni476 – 4816Combined sources
    Helixi484 – 49411Combined sources
    Helixi507 – 51711Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O6YX-ray1.50A/B/C/D/E/F/G/H1-523[»]
    2O78X-ray1.90A/B/C/D/E/F/G/H1-523[»]
    2O7BX-ray1.60A/B/C/D/E/F/G/H1-523[»]
    2O7DX-ray1.90A/B/C/D/E/F/G/H1-523[»]
    2O7EX-ray1.75A/B/C/D/E/F/G/H1-523[»]
    2O7FX-ray2.00A/B/C/D/E/F/G/H1-523[»]
    ProteinModelPortaliQ3IWB0.
    SMRiQ3IWB0. Positions 7-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ3IWB0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni432 – 4365Substrate binding

    Sequence similaritiesi

    Belongs to the PAL/histidase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C84. Bacteria.
    COG2986. LUCA.
    HOGENOMiHOG000237620.
    KOiK10774.
    OMAiLTPLAHM.
    OrthoDBiEOG62K1W2.
    PhylomeDBiQ3IWB0.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    InterProiIPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    [Graphical view]
    PfamiPF00221. Lyase_aromatic. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3IWB0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLAMSPPKPA VELDRHIDLD QAHAVASGGA RIVLAPPARD RCRASEARLG
    60 70 80 90 100
    AVIREARHVY GLTTGFGPLA NRLISGENVR TLQANLVHHL ASGVGPVLDW
    110 120 130 140 150
    TTARAMVLAR LVSIAQGASG ASEGTIARLI DLLNSELAPA VPSRGTVGAS
    160 170 180 190 200
    GDLTPLAHMV LCLQGRGDFL DRDGTRLDGA EGLRRGRLQP LDLSHRDALA
    210 220 230 240 250
    LVNGTSAMTG IALVNAHACR HLGNWAVALT ALLAECLRGR TEAWAAALSD
    260 270 280 290 300
    LRPHPGQKDA AARLRARVDG SARVVRHVIA ERRLDAGDIG TEPEAGQDAY
    310 320 330 340 350
    SLRCAPQVLG AGFDTLAWHD RVLTIELNAV TDNPVFPPDG SVPALHGGNF
    360 370 380 390 400
    MGQHVALTSD ALATAVTVLA GLAERQIARL TDERLNRGLP PFLHRGPAGL
    410 420 430 440 450
    NSGFMGAQVT ATALLAEMRA TGPASIHSIS TNAANQDVVS LGTIAARLCR
    460 470 480 490 500
    EKIDRWAEIL AILALCLAQA AELRCGSGLD GVSPAGKKLV QALREQFPPL
    510 520
    ETDRPLGQEI AALATHLLQQ SPV
    Length:523
    Mass (Da):54,914
    Last modified:November 8, 2005 - v1
    Checksum:iED77FA23DB0540B9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000144 Genomic DNA. Translation: ABA81174.1.
    RefSeqiWP_011339422.1. NZ_AKVW01000002.1.
    YP_355075.1. NC_007494.2.

    Genome annotation databases

    EnsemblBacteriaiABA81174; ABA81174; RSP_3574.
    GeneIDi3722088.
    KEGGirsp:RSP_3574.
    PATRICi23157331. VBIRhoSph57909_4010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000144 Genomic DNA. Translation: ABA81174.1.
    RefSeqiWP_011339422.1. NZ_AKVW01000002.1.
    YP_355075.1. NC_007494.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O6YX-ray1.50A/B/C/D/E/F/G/H1-523[»]
    2O78X-ray1.90A/B/C/D/E/F/G/H1-523[»]
    2O7BX-ray1.60A/B/C/D/E/F/G/H1-523[»]
    2O7DX-ray1.90A/B/C/D/E/F/G/H1-523[»]
    2O7EX-ray1.75A/B/C/D/E/F/G/H1-523[»]
    2O7FX-ray2.00A/B/C/D/E/F/G/H1-523[»]
    ProteinModelPortaliQ3IWB0.
    SMRiQ3IWB0. Positions 7-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272943.RSP_3574.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABA81174; ABA81174; RSP_3574.
    GeneIDi3722088.
    KEGGirsp:RSP_3574.
    PATRICi23157331. VBIRhoSph57909_4010.

    Phylogenomic databases

    eggNOGiENOG4105C84. Bacteria.
    COG2986. LUCA.
    HOGENOMiHOG000237620.
    KOiK10774.
    OMAiLTPLAHM.
    OrthoDBiEOG62K1W2.
    PhylomeDBiQ3IWB0.

    Enzyme and pathway databases

    BioCyciRSPH272943:GJAS-3700-MONOMER.
    SABIO-RKQ3IWB0.

    Miscellaneous databases

    EvolutionaryTraceiQ3IWB0.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    InterProiIPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    [Graphical view]
    PfamiPF00221. Lyase_aromatic. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
    2. "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases."
      Louie G.V., Bowman M.E., Moffitt M.C., Baiga T.J., Moore B.S., Noel J.P.
      Chem. Biol. 13:1327-1338(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF WILD-TYPE AND MUTANT PHE-89 IN COMPLEXES WITH CINNAMAT; P-COUMARATE AND CAFFEATE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, SUBUNIT.

    Entry informationi

    Entry nameiTALY_RHOS4
    AccessioniPrimary (citable) accession number: Q3IWB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: November 8, 2005
    Last modified: December 9, 2015
    This is version 74 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, Complete proteome, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.