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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: -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

    • 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

    Keywordsi

    Molecular functionLyase
    Biological processPhenylpropanoid metabolism

    Enzyme and pathway databases

    SABIO-RKiQ3IWB0

    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

    Chemistry databases

    DrugBankiDB04066 Para-Coumaric Acid

    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)1 Publication
    Modified residuei1502,3-didehydroalanine (Ser)1 Publication1

    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

    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
    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
    OMAiMLTRCNS
    OrthoDBiPOG091H04Z2
    PhylomeDBiQ3IWB0

    Family and domain databases

    CDDicd00332 PAL-HAL, 1 hit
    Gene3Di1.10.275.10, 1 hit
    InterProiView protein in InterPro
    IPR001106 Aromatic_Lyase
    IPR024083 Fumarase/histidase_N
    IPR008948 L-Aspartase-like
    IPR022313 Phe/His_NH3-lyase_AS
    PANTHERiPTHR10362 PTHR10362, 1 hit
    PfamiView protein in Pfam
    PF00221 Lyase_aromatic, 1 hit
    SUPFAMiSSF48557 SSF48557, 1 hit
    PROSITEiView protein in PROSITE
    PS00488 PAL_HISTIDASE, 1 hit

    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
    PATRICifig|272943.9.peg.4010

    Similar proteinsi

    Entry informationi

    Entry nameiTALY_RHOS4
    AccessioniPrimary (citable) accession number: Q3IWB0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: November 8, 2005
    Last modified: January 31, 2018
    This is version 83 of the entry and version 1 of the sequence. See 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

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