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P21310

- HUTH_PSEPU

UniProt

P21310 - HUTH_PSEPU

Protein

Histidine ammonia-lyase

Gene

hutH

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-histidine = urocanate + NH3.4 Publications

    Pathwayi

    GO - Molecular functioni

    1. histidine ammonia-lyase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. biosynthetic process Source: InterPro
    2. histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
    3. histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Histidine metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11608.
    UniPathwayiUPA00379; UER00549.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine ammonia-lyase (EC:4.3.1.3)
    Short name:
    Histidase
    Gene namesi
    Name:hutH
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi113 – 1131S → A: No loss of activity.
    Mutagenesisi144 – 1441S → A or T: Complete loss of activity. 3 Publications
    Mutagenesisi144 – 1441S → C: No effect. 3 Publications
    Mutagenesisi394 – 3941S → A: No loss of activity.
    Mutagenesisi419 – 4191S → A: No loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 510509Histidine ammonia-lyasePRO_0000161017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki143 ↔ 1455-imidazolinone (Ala-Gly)
    Modified residuei144 – 14412,3-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.

    Expressioni

    Inductioni

    By histidine and urocanate.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    510
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Helixi13 – 219
    Beta strandi25 – 284
    Helixi30 – 323
    Helixi33 – 4816
    Turni54 – 563
    Helixi61 – 633
    Helixi70 – 8415
    Beta strandi88 – 914
    Helixi94 – 10815
    Turni109 – 1124
    Helixi117 – 12913
    Beta strandi131 – 1333
    Beta strandi136 – 1383
    Beta strandi142 – 1454
    Helixi147 – 1559
    Helixi156 – 1583
    Beta strandi161 – 1655
    Beta strandi168 – 1714
    Helixi172 – 1787
    Helixi190 – 1956
    Beta strandi196 – 1983
    Helixi199 – 22931
    Helixi235 – 2373
    Helixi239 – 2457
    Helixi248 – 26114
    Helixi266 – 2705
    Turni271 – 2733
    Helixi274 – 2763
    Helixi281 – 2844
    Helixi286 – 30823
    Beta strandi314 – 3185
    Turni319 – 3224
    Beta strandi323 – 3253
    Helixi333 – 36129
    Helixi363 – 3664
    Helixi370 – 3723
    Turni376 – 3783
    Helixi383 – 39917
    Turni411 – 4144
    Helixi421 – 45131
    Helixi460 – 47011
    Beta strandi478 – 4803
    Helixi483 – 49412
    Turni495 – 4984
    Helixi499 – 5013
    Beta strandi504 – 5074

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B8FX-ray2.10A2-510[»]
    1EB4X-ray2.00A2-510[»]
    1GK2X-ray1.90A/B/C/D2-510[»]
    1GK3X-ray2.25A2-510[»]
    1GKJX-ray1.70A2-510[»]
    1GKMX-ray1.00A2-510[»]
    ProteinModelPortaliP21310.
    SMRiP21310. Positions 2-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21310.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PAL/histidase family.Curated

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00229. His_ammonia_lyase.
    InterProiIPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR005921. HutH.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    [Graphical view]
    PfamiPF00221. Lyase_aromatic. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR01225. hutH. 1 hit.
    PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P21310-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED    50
    RTAYGINTGF GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI 100
    MVLKINSLSR GFSGIRRKVI DALIALVNAE VYPHIPLKGS VGASGDLAPL 150
    AHMSLVLLGE GKARYKGQWL SATEALAVAG LEPLTLAAKE GLALLNGTQA 200
    STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR IHEARGQRGQ 250
    IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA 300
    AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG 350
    SLSERRISLM MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS 400
    HPHSVDSLPT SANQEDHVSM APAAGKRLWE MAENTRGVLA IEWLGACQGL 450
    DLRKGLKTSA KLEKARQALR SEVAHYDRDR FFAPDIEKAV ELLAKGSLTG 500
    LLPAGVLPSL 510
    Length:510
    Mass (Da):53,761
    Last modified:January 23, 2007 - v3
    Checksum:i7D80C7E64B0C4F57
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521H → T in AAA25840. (PubMed:2332400)Curated
    Sequence conflicti439 – 4391L → P in AAA25840. (PubMed:2332400)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35140 Genomic DNA. Translation: AAA25840.1.
    PIRiA35251.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35140 Genomic DNA. Translation: AAA25840.1 .
    PIRi A35251.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B8F X-ray 2.10 A 2-510 [» ]
    1EB4 X-ray 2.00 A 2-510 [» ]
    1GK2 X-ray 1.90 A/B/C/D 2-510 [» ]
    1GK3 X-ray 2.25 A 2-510 [» ]
    1GKJ X-ray 1.70 A 2-510 [» ]
    1GKM X-ray 1.00 A 2-510 [» ]
    ProteinModelPortali P21310.
    SMRi P21310. Positions 2-510.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00379 ; UER00549 .
    BioCyci MetaCyc:MONOMER-11608.

    Miscellaneous databases

    EvolutionaryTracei P21310.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    HAMAPi MF_00229. His_ammonia_lyase.
    InterProi IPR001106. Aromatic_Lyase.
    IPR024083. Fumarase/histidase_N.
    IPR005921. HutH.
    IPR008948. L-Aspartase-like.
    IPR022313. Phe/His_NH3-lyase_AS.
    [Graphical view ]
    Pfami PF00221. Lyase_aromatic. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR01225. hutH. 1 hit.
    PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida."
      Consevage M.W., Phillips A.T.
      J. Bacteriol. 172:2224-2229(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
      Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
    2. "Identification of Ser143 as the site of modification in the active site of histidine ammonia-lyase."
      Hernandez D., Stroh J.G., Phillips A.T.
      Arch. Biochem. Biophys. 307:126-132(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, IDENTIFICATION BY MASS SPECTROMETRY.
    3. "Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida."
      Hernandez D., Phillips A.T.
      Biochem. Biophys. Res. Commun. 201:1433-1438(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, MUTAGENESIS OF SER-144.
    4. "Identification of serine-143 as the most likely precursor of dehydroalanine in the active site of histidine ammonia-lyase. A study of the overexpressed enzyme by site-directed mutagenesis."
      Langer M., Reck G., Reed J., Retey J.
      Biochemistry 33:6462-6467(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDROALANINE FORMATION, MUTAGENESIS OF SER-144.
    5. "Histidine ammonia-lyase mutant S143C is posttranslationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine."
      Langer M., Lieber A., Retey J.
      Biochemistry 33:14034-14038(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, MUTAGENESIS OF SER-144.
    6. "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile."
      Schwede T.F., Retey J., Schulz G.E.
      Biochemistry 38:5355-5361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 152 AND 439.
      Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.

    Entry informationi

    Entry nameiHUTH_PSEPU
    AccessioniPrimary (citable) accession number: P21310
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 104 of the entry and version 3 of the sequence. [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

    External Data

    Dasty 3