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P13449

- NHAB_RHOER

UniProt

P13449 - NHAB_RHOER

Protein

Nitrile hydratase subunit beta

Gene

nthB

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.

    Catalytic activityi

    An aliphatic amide = a nitrile + H2O.

    GO - Molecular functioni

    1. indole-3-acetonitrile nitrile hydratase activity Source: UniProtKB-EC
    2. transition metal ion binding Source: InterPro

    GO - Biological processi

    1. nitrogen compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    SABIO-RKP13449.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitrile hydratase subunit beta (EC:4.2.1.84)
    Short name:
    NHase
    Short name:
    Nitrilase
    Gene namesi
    Name:nthB
    Synonyms:nha2
    OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
    Taxonomic identifieri1833 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

    Pathology & Biotechi

    Biotechnological usei

    Industrial production of acrylamide is now being developed using some of these enzymes.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 212212Nitrile hydratase subunit betaPRO_0000186831Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    DIPiDIP-6076N.

    Structurei

    Secondary structure

    1
    212
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni31 – 344
    Helixi35 – 4511
    Helixi52 – 609
    Helixi64 – 696
    Helixi72 – 8615
    Helixi92 – 998
    Beta strandi128 – 1314
    Helixi144 – 1463
    Beta strandi150 – 1567
    Helixi164 – 1674
    Turni168 – 1703
    Beta strandi179 – 1857
    Helixi186 – 1905
    Beta strandi197 – 2048
    Helixi205 – 2073
    Beta strandi208 – 2103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AHJX-ray2.65B/D/F/H1-212[»]
    2AHJX-ray1.70B/D1-212[»]
    2CYZX-ray1.55B1-212[»]
    2CZ0X-ray1.50B1-212[»]
    2CZ1X-ray1.39B1-212[»]
    2CZ6X-ray1.50B1-212[»]
    2CZ7X-ray1.80B1-212[»]
    2D0QX-ray1.65B1-212[»]
    2QDYX-ray1.30B1-212[»]
    2ZCFX-ray1.43B1-212[»]
    2ZPBX-ray1.30B1-212[»]
    2ZPEX-ray1.48B1-212[»]
    2ZPFX-ray1.48B1-212[»]
    2ZPGX-ray1.39B1-212[»]
    2ZPHX-ray1.59B1-212[»]
    2ZPIX-ray1.49B1-212[»]
    3A8GX-ray1.11B1-212[»]
    3A8HX-ray1.66B1-212[»]
    3A8LX-ray1.63B1-212[»]
    3A8MX-ray1.32B1-212[»]
    3A8OX-ray1.47B1-212[»]
    ProteinModelPortaliP13449.
    SMRiP13449. Positions 1-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13449.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR024690. CN_hydtase_beta_dom.
    IPR008990. Elect_transpt_acc-like_dom.
    IPR003168. Nitrile_hydratase_bsu.
    [Graphical view]
    PfamiPF02211. NHase_beta. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001427. NHase_beta. 1 hit.
    SUPFAMiSSF50090. SSF50090. 1 hit.
    TIGRFAMsiTIGR03888. nitrile_beta. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P13449-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGVHDLAGV QGFGKVPHTV NADIGPTFHA EWEHLPYSLM FAGVAELGAF    50
    SVDEVRYVVE RMEPRHYMMT PYYERYVIGV ATLMVEKGIL TQDELESLAG 100
    GPFPLSRPSE SEGRPAPVET TTFEVGQRVR VRDEYVPGHI RMPAYCRGRV 150
    GTISHRTTEK WPFPDAIGHG RNDAGEEPTY HVKFAAEELF GSDTDGGSVV 200
    VDLFEGYLEP AA 212
    Length:212
    Mass (Da):23,487
    Last modified:January 1, 1990 - v1
    Checksum:iA0401CA4FC1C2CBE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401M → V in strain: ACV2.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54074 Genomic DNA. Translation: CAA38011.1.
    X14668 Genomic DNA. Translation: CAA32798.1.
    Z48769 Genomic DNA. Translation: CAA88686.1.
    AB016078 Genomic DNA. Translation: BAA36598.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54074 Genomic DNA. Translation: CAA38011.1 .
    X14668 Genomic DNA. Translation: CAA32798.1 .
    Z48769 Genomic DNA. Translation: CAA88686.1 .
    AB016078 Genomic DNA. Translation: BAA36598.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AHJ X-ray 2.65 B/D/F/H 1-212 [» ]
    2AHJ X-ray 1.70 B/D 1-212 [» ]
    2CYZ X-ray 1.55 B 1-212 [» ]
    2CZ0 X-ray 1.50 B 1-212 [» ]
    2CZ1 X-ray 1.39 B 1-212 [» ]
    2CZ6 X-ray 1.50 B 1-212 [» ]
    2CZ7 X-ray 1.80 B 1-212 [» ]
    2D0Q X-ray 1.65 B 1-212 [» ]
    2QDY X-ray 1.30 B 1-212 [» ]
    2ZCF X-ray 1.43 B 1-212 [» ]
    2ZPB X-ray 1.30 B 1-212 [» ]
    2ZPE X-ray 1.48 B 1-212 [» ]
    2ZPF X-ray 1.48 B 1-212 [» ]
    2ZPG X-ray 1.39 B 1-212 [» ]
    2ZPH X-ray 1.59 B 1-212 [» ]
    2ZPI X-ray 1.49 B 1-212 [» ]
    3A8G X-ray 1.11 B 1-212 [» ]
    3A8H X-ray 1.66 B 1-212 [» ]
    3A8L X-ray 1.63 B 1-212 [» ]
    3A8M X-ray 1.32 B 1-212 [» ]
    3A8O X-ray 1.47 B 1-212 [» ]
    ProteinModelPortali P13449.
    SMRi P13449. Positions 1-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6076N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P13449.

    Miscellaneous databases

    EvolutionaryTracei P13449.

    Family and domain databases

    InterProi IPR024690. CN_hydtase_beta_dom.
    IPR008990. Elect_transpt_acc-like_dom.
    IPR003168. Nitrile_hydratase_bsu.
    [Graphical view ]
    Pfami PF02211. NHase_beta. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001427. NHase_beta. 1 hit.
    SUPFAMi SSF50090. SSF50090. 1 hit.
    TIGRFAMsi TIGR03888. nitrile_beta. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of nitrile hydratase deduced from the nucleotide sequence of a Rhodococcus species and its expression in Escherichia coli."
      Ikehata O., Nishiyama M., Horinouchi S., Beppu T.
      Eur. J. Biochem. 181:563-570(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: N-774.
    2. "Cloning and characterization of an amidase gene from Rhodococcus species N-774 and its expression in Escherichia coli."
      Hashimoto Y., Nishiyama M., Ikehata O., Horinouchi S., Beppu T.
      Biochim. Biophys. Acta 1088:225-233(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: N-774.
    3. Bigey F., Chebrou H., Arnaud A., Galzy P.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ACV2.
    4. "Functional expression of nitrile hydratase in Escherichia coli: requirement of a nitrile hydratase activator and post-translational modification of a ligand cysteine."
      Nojiri M., Yohda M., Odaka M., Matsushita Y., Tsujimura M., Yoshida T., Dohmae N., Takio K., Endo I.
      J. Biochem. 125:696-704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: N-771.
    5. "Nitrile hydratase of Rhodococcus sp. N-774. Purification and amino acid sequences."
      Endo T., Watanabe I.
      FEBS Lett. 243:61-64(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-19.
      Strain: N-774.
    6. "Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold."
      Huang W., Jia J., Cummings J., Nelson M., Schneider G., Lindqvist Y.
      Structure 5:691-699(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
      Strain: Brevibacterium sp. R312.
    7. "Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms."
      Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K., Odaka M., Yohda M., Kamiya N., Endo I.
      Nat. Struct. Biol. 5:347-351(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiNHAB_RHOER
    AccessioniPrimary (citable) accession number: P13449
    Secondary accession number(s): Q59789
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 86 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, Direct protein sequencing

    Documents

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

    External Data

    Dasty 3