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Protein

Urocanate hydratase

Gene

hutU

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.UniRule annotation1 Publication

Catalytic activityi

3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O.UniRule annotation1 Publication

Cofactori

NAD+UniRule annotation3 PublicationsNote: Binds 1 NAD+ per subunit.UniRule annotation2 Publications

Kineticsi

  1. KM=35.4 µM for urucanate1 Publication

    Pathwayi: L-histidine degradation into L-glutamate

    This protein is involved in step 2 of the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Histidine ammonia-lyase (DW66_2585), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (SAMN03097715_02348), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (PU99_10260), Histidine ammonia-lyase (hutH_2), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (BIW19_01715), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (HA62_16700), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (HB13667_15065), Histidine ammonia-lyase (hutH_3), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH_1), Histidine ammonia-lyase (HB4184_14930), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (AYO28_15945)
    2. Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (BIW19_25300), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU)
    3. Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI)
    This subpathway is part of the pathway L-histidine degradation into L-glutamate, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine, the pathway L-histidine degradation into L-glutamate and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei131NADUniRule annotationCombined sources2 Publications1
    Active sitei411UniRule annotation1 Publication1
    Binding sitei493NAD; via carbonyl oxygenUniRule annotationCombined sources2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi53 – 54NADUniRule annotationCombined sources2 Publications2
    Nucleotide bindingi177 – 179NADUniRule annotationCombined sources2 Publications3
    Nucleotide bindingi197 – 202NADCombined sources2 Publications6
    Nucleotide bindingi243 – 244NADUniRule annotationCombined sources2 Publications2
    Nucleotide bindingi264 – 268NADUniRule annotationCombined sources2 Publications5
    Nucleotide bindingi274 – 275NADUniRule annotationCombined sources2 Publications2
    Nucleotide bindingi323 – 324NADCombined sources2 Publications2
    Nucleotide bindingi455 – 456NADCombined sources2 Publications2

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    Biological processHistidine metabolism
    LigandNAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11616.
    BRENDAi4.2.1.49. 5092.
    UniPathwayiUPA00379; UER00550.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urocanate hydrataseUniRule annotation (EC:4.2.1.49UniRule annotation1 Publication)
    Short name:
    Urocanase1 PublicationUniRule annotation
    Alternative name(s):
    Imidazolonepropionate hydrolaseUniRule annotation
    Gene namesi
    Name:hutU1 PublicationUniRule annotation
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi64C → A: No loss of activity. 1 Publication1
    Mutagenesisi192C → A: No loss of activity. 1 Publication1
    Mutagenesisi198C → A: No loss of activity. 1 Publication1
    Mutagenesisi355C → A: Minor loss in activity. 1 Publication1
    Mutagenesisi411C → A: Loss of activity. 1 Publication1
    Mutagenesisi544C → A: No loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00002073442 – 557Urocanate hydrataseAdd BLAST556

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1557
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi21 – 24Combined sources4
    Helixi25 – 37Combined sources13
    Turni40 – 42Combined sources3
    Helixi46 – 48Combined sources3
    Beta strandi50 – 52Combined sources3
    Turni53 – 55Combined sources3
    Beta strandi56 – 61Combined sources6
    Helixi62 – 74Combined sources13
    Beta strandi79 – 84Combined sources6
    Beta strandi87 – 93Combined sources7
    Beta strandi100 – 106Combined sources7
    Helixi110 – 112Combined sources3
    Helixi115 – 123Combined sources9
    Turni131 – 137Combined sources7
    Helixi143 – 160Combined sources18
    Beta strandi161 – 163Combined sources3
    Beta strandi169 – 173Combined sources5
    Turni177 – 180Combined sources4
    Helixi181 – 188Combined sources8
    Beta strandi192 – 198Combined sources7
    Helixi200 – 208Combined sources9
    Helixi219 – 231Combined sources13
    Beta strandi237 – 242Combined sources6
    Helixi244 – 254Combined sources11
    Beta strandi259 – 261Combined sources3
    Turni270 – 272Combined sources3
    Helixi281 – 290Combined sources10
    Helixi292 – 315Combined sources24
    Helixi327 – 333Combined sources7
    Helixi339 – 341Combined sources3
    Helixi345 – 348Combined sources4
    Helixi351 – 354Combined sources4
    Turni355 – 357Combined sources3
    Beta strandi361 – 365Combined sources5
    Helixi370 – 383Combined sources14
    Helixi388 – 400Combined sources13
    Beta strandi408 – 410Combined sources3
    Helixi417 – 430Combined sources14
    Beta strandi433 – 436Combined sources4
    Beta strandi438 – 442Combined sources5
    Beta strandi449 – 451Combined sources3
    Turni453 – 459Combined sources7
    Helixi469 – 481Combined sources13
    Beta strandi484 – 491Combined sources8
    Turni492 – 494Combined sources3
    Beta strandi500 – 508Combined sources9
    Helixi512 – 535Combined sources24
    Helixi539 – 547Combined sources9
    Turni553 – 555Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1UWKX-ray1.19A/B1-557[»]
    1UWLX-ray1.76A/B1-557[»]
    1W1UX-ray2.23A/B2-557[»]
    2V7GX-ray2.00A/B/C/D2-557[»]
    ProteinModelPortaliP25080.
    SMRiP25080.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25080.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the urocanase family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105CGP. Bacteria.
    COG2987. LUCA.

    Family and domain databases

    HAMAPiMF_00577. HutU. 1 hit.
    InterProiView protein in InterPro
    IPR023637. Urocanase.
    IPR035401. Urocanase_C.
    IPR023636. Urocanase_CS.
    IPR035400. Urocanase_N.
    IPR035085. Urocanase_Rossmann-like.
    IPR036190. Urocanase_sf.
    PANTHERiPTHR12216. PTHR12216. 1 hit.
    PfamiView protein in Pfam
    PF01175. Urocanase. 1 hit.
    PF17392. Urocanase_C. 1 hit.
    PF17391. Urocanase_N. 1 hit.
    PIRSFiPIRSF001423. Urocanate_hydrat. 1 hit.
    SUPFAMiSSF111326. SSF111326. 1 hit.
    TIGRFAMsiTIGR01228. hutU. 1 hit.
    PROSITEiView protein in PROSITE
    PS01233. UROCANASE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25080-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDNNKYRDV EIRAPRGNKL TAKSWLTEAP LRMLMNNLDP QVAENPKELV
    60 70 80 90 100
    VYGGIGRAAR NWECYDKIVE TLTRLEDDET LLVQSGKPVG VFKTHSNAPR
    110 120 130 140 150
    VLIANSNLVP HWANWEHFNE LDAKGLAMYG QMTAGSWIYI GSQGIVQGTY
    160 170 180 190 200
    ETFVEAGRQH YGGTVKAKWV LTAGLGGMGG AQPLAATLAG ACSLNIECQQ
    210 220 230 240 250
    SRIDFRLETR YVDEQATDLD DALVRIAKYT AEGKAISIAL HGNAAEILPE
    260 270 280 290 300
    LVKRGVRPDM VTDQTSAHDP LNGYLPAGWT WEQYRDRAQT EPAAVVKAAK
    310 320 330 340 350
    QSMAVHVQAM LDFQKQGVPT FDYGNNIRQM AKEEGVANAF DFPGFVPAYI
    360 370 380 390 400
    RPLFCRGVGP FRWAALSGEA EDIYKTDAKV KELIPDDAHL HRWLDMARER
    410 420 430 440 450
    ISFQGLPARI CWVGLGLRAK LGLAFNEMVR SGELSAPVVI GRDHLDSGSV
    460 470 480 490 500
    SSPNRETEAM RDGSDAVSDW PLLNALLNTA GGATWVSLHH GGGVGMGFSQ
    510 520 530 540 550
    HSGMVIVCDG TDEAAERIAR VLTNDPGTGV MRHADAGYDI AIDCAKEQGL

    DLPMITG
    Length:557
    Mass (Da):60,804
    Last modified:January 23, 2007 - v2
    Checksum:i5AFD1E3307F34434
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti164 – 167TVKA → SLKG in AAA50311 (Ref. 2) Curated4

    Mass spectrometryi

    Molecular mass is 60686±15 Da from positions 2 - 557. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X58483 Genomic DNA. Translation: CAA41392.1.
    M33923 Genomic DNA. Translation: AAA50311.1.
    PIRiS17184. DWPSUP.
    T45008.

    Similar proteinsi

    Entry informationi

    Entry nameiHUTU_PSEPU
    AccessioniPrimary (citable) accession number: P25080
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: November 22, 2017
    This is version 113 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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