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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)DescriptionActionsGraphical viewLength
    Active sitei60Proton donor/acceptorBy similarity1
    Binding sitei89Substrate1
    Binding sitei303Substrate1

    GO - Molecular functioni

    • 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

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi89H → F: Abolishes tyrosine ammonia-lyase activity. Increases affinity for L-Phe. Increases the low intrinsic phenylalanine ammonia-lyase activity about twentyfold. 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004299681 – 523Tyrosine ammonia-lyaseAdd BLAST523

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki149 ↔ 1515-imidazolinone (Ala-Gly)
    Modified residuei1502,3-didehydroalanine (Ser)1

    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

    Protein-protein interaction databases

    STRINGi272943.RSP_3574.

    Structurei

    Secondary structure

    1523
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 15Combined sources6
    Helixi19 – 26Combined sources8
    Beta strandi29 – 34Combined sources6
    Helixi36 – 54Combined sources19
    Turni60 – 62Combined sources3
    Helixi67 – 71Combined sources5
    Helixi76 – 78Combined sources3
    Helixi79 – 90Combined sources12
    Beta strandi94 – 97Combined sources4
    Helixi100 – 114Combined sources15
    Helixi123 – 133Combined sources11
    Beta strandi142 – 144Combined sources3
    Beta strandi148 – 151Combined sources4
    Helixi153 – 163Combined sources11
    Helixi179 – 185Combined sources7
    Helixi198 – 200Combined sources3
    Beta strandi203 – 205Combined sources3
    Helixi206 – 236Combined sources31
    Helixi241 – 244Combined sources4
    Helixi246 – 251Combined sources6
    Helixi255 – 267Combined sources13
    Turni268 – 270Combined sources3
    Beta strandi272 – 275Combined sources4
    Helixi279 – 281Combined sources3
    Helixi286 – 288Combined sources3
    Helixi300 – 303Combined sources4
    Helixi305 – 327Combined sources23
    Beta strandi333 – 335Combined sources3
    Beta strandi341 – 343Combined sources3
    Helixi353 – 380Combined sources28
    Turni383 – 388Combined sources6
    Helixi391 – 393Combined sources3
    Beta strandi396 – 398Combined sources3
    Helixi405 – 419Combined sources15
    Helixi425 – 427Combined sources3
    Turni432 – 435Combined sources4
    Helixi442 – 475Combined sources34
    Turni476 – 481Combined sources6
    Helixi484 – 494Combined sources11
    Helixi507 – 517Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ3IWB0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni432 – 436Substrate binding5

    Sequence similaritiesi

    Belongs to the PAL/histidase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C84. Bacteria.
    COG2986. LUCA.
    HOGENOMiHOG000237620.
    KOiK10774.
    OMAiLTPLAHM.
    OrthoDBiPOG091H04Z2.
    PhylomeDBiQ3IWB0.

    Family and domain databases

    CDDicd00332. PAL-HAL. 1 hit.
    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
    PDB 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.
    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.
    OrthoDBiPOG091H04Z2.
    PhylomeDBiQ3IWB0.

    Enzyme and pathway databases

    SABIO-RKQ3IWB0.

    Miscellaneous databases

    EvolutionaryTraceiQ3IWB0.

    Family and domain databases

    CDDicd00332. PAL-HAL. 1 hit.
    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...

    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: November 2, 2016
    This is version 77 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.