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P13448

- NHAA_RHOER

UniProt

P13448 - NHAA_RHOER

Protein

Nitrile hydratase subunit alpha

Gene

nthA

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class.

    Catalytic activityi

    An aliphatic amide = a nitrile + H2O.

    Cofactori

    Binds 1 Fe3+ ion per subunit.

    Enzyme regulationi

    Inactivated by nitrosylation of the iron center in the dark and activated by photo-induced nitric oxide (NO) release. Inactivated by oxidation of Cys-115 to a sulfenic acid.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi110 – 1101Iron
    Metal bindingi113 – 1131Iron
    Metal bindingi114 – 1141Iron
    Metal bindingi115 – 1151Iron

    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

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP13448.

    Names & Taxonomyi

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 207206Nitrile hydratase subunit alphaPRO_0000186823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei113 – 1131Cysteine sulfinic acid (-SO2H)2 Publications
    Modified residuei115 – 1151Cysteine sulfenic acid (-SOH)1 Publication

    Post-translational modificationi

    Oxidation on Cys-113 is essential for the activity.2 Publications
    Oxidation on Cys-115 stabilizes the Fe-NO ligand coordinated in the inactive form.1 Publication

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    DIPiDIP-6075N.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 3113
    Turni32 – 343
    Helixi40 – 5011
    Helixi54 – 6613
    Helixi68 – 769
    Helixi78 – 847
    Beta strandi92 – 998
    Beta strandi104 – 1096
    Helixi118 – 1214
    Helixi126 – 1294
    Helixi131 – 1366
    Turni137 – 1393
    Helixi141 – 1488
    Beta strandi156 – 1627
    Beta strandi165 – 1728
    Helixi184 – 1907
    Helixi193 – 1975
    Beta strandi198 – 2003

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AHJX-ray2.65A/C/E/G1-207[»]
    2AHJX-ray1.70A/C2-207[»]
    2CYZX-ray1.55A2-207[»]
    2CZ0X-ray1.50A2-207[»]
    2CZ1X-ray1.39A2-207[»]
    2CZ6X-ray1.50A2-207[»]
    2CZ7X-ray1.80A2-207[»]
    2D0QX-ray1.65A2-207[»]
    2QDYX-ray1.30A1-207[»]
    2ZCFX-ray1.43A2-207[»]
    2ZPBX-ray1.30A2-207[»]
    2ZPEX-ray1.48A2-207[»]
    2ZPFX-ray1.48A2-207[»]
    2ZPGX-ray1.39A2-207[»]
    2ZPHX-ray1.59A2-207[»]
    2ZPIX-ray1.49A2-207[»]
    3A8GX-ray1.11A1-207[»]
    3A8HX-ray1.66A1-207[»]
    3A8LX-ray1.63A1-207[»]
    3A8MX-ray1.32A1-207[»]
    3A8OX-ray1.47A1-207[»]
    ProteinModelPortaliP13448.
    SMRiP13448. Positions 10-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13448.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.90.330.10. 1 hit.
    InterProiIPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
    IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
    IPR018141. Nitrile_hydratase_asu.
    [Graphical view]
    PfamiPF02979. NHase_alpha. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001426. NHase_alpha. 1 hit.
    ProDomiPD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF56209. SSF56209. 1 hit.
    TIGRFAMsiTIGR01323. nitrile_alph. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P13448-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVTIDHTTE NAAPAQAPVS DRAWALFRAL DGKGLVPDGY VEGWKKTFEE    50
    DFSPRRGAEL VARAWTDPEF RQLLLTDGTA AVAQYGYLGP QGEYIVAVED 100
    TPTLKNVIVC SLCSCTAWPI LGLPPTWYKS FEYRARVVRE PRKVLSEMGT 150
    EIASDIEIRV YDTTAETRYM VLPQRPAGTE GWSQEQLQEI VTKDCLIGVA 200
    IPQVPTV 207
    Length:207
    Mass (Da):22,996
    Last modified:January 23, 2007 - v3
    Checksum:i22DD21260A2D70E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181P → A AA sequence (PubMed:2659343)Curated
    Sequence conflicti20 – 201S → T AA sequence (PubMed:2920826)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14668 Genomic DNA. Translation: CAA32797.1.
    X54074 Genomic DNA. Translation: CAA38010.1.
    Z48769 Genomic DNA. Translation: CAA88685.1.
    AB016078 Genomic DNA. Translation: BAA36597.1.
    M60264 Genomic DNA. Translation: AAA62722.1.
    PIRiB37806.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14668 Genomic DNA. Translation: CAA32797.1 .
    X54074 Genomic DNA. Translation: CAA38010.1 .
    Z48769 Genomic DNA. Translation: CAA88685.1 .
    AB016078 Genomic DNA. Translation: BAA36597.1 .
    M60264 Genomic DNA. Translation: AAA62722.1 .
    PIRi B37806.

    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 A/C/E/G 1-207 [» ]
    2AHJ X-ray 1.70 A/C 2-207 [» ]
    2CYZ X-ray 1.55 A 2-207 [» ]
    2CZ0 X-ray 1.50 A 2-207 [» ]
    2CZ1 X-ray 1.39 A 2-207 [» ]
    2CZ6 X-ray 1.50 A 2-207 [» ]
    2CZ7 X-ray 1.80 A 2-207 [» ]
    2D0Q X-ray 1.65 A 2-207 [» ]
    2QDY X-ray 1.30 A 1-207 [» ]
    2ZCF X-ray 1.43 A 2-207 [» ]
    2ZPB X-ray 1.30 A 2-207 [» ]
    2ZPE X-ray 1.48 A 2-207 [» ]
    2ZPF X-ray 1.48 A 2-207 [» ]
    2ZPG X-ray 1.39 A 2-207 [» ]
    2ZPH X-ray 1.59 A 2-207 [» ]
    2ZPI X-ray 1.49 A 2-207 [» ]
    3A8G X-ray 1.11 A 1-207 [» ]
    3A8H X-ray 1.66 A 1-207 [» ]
    3A8L X-ray 1.63 A 1-207 [» ]
    3A8M X-ray 1.32 A 1-207 [» ]
    3A8O X-ray 1.47 A 1-207 [» ]
    ProteinModelPortali P13448.
    SMRi P13448. Positions 10-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6075N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P13448.

    Miscellaneous databases

    EvolutionaryTracei P13448.

    Family and domain databases

    Gene3Di 3.90.330.10. 1 hit.
    InterProi IPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
    IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
    IPR018141. Nitrile_hydratase_asu.
    [Graphical view ]
    Pfami PF02979. NHase_alpha. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001426. NHase_alpha. 1 hit.
    ProDomi PD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF56209. SSF56209. 1 hit.
    TIGRFAMsi TIGR01323. nitrile_alph. 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. "Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase."
      Mayaux J.-F., Cerbelaud E., Soubrier F., Faucher D., Petre D.
      J. Bacteriol. 172:6764-6773(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
      Strain: Brevibacterium sp. R312.
    6. "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 2-20.
      Strain: N-774.
    7. "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.
    8. "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, OXIDATION AT CYS-113 AND CYS-115, LIGAND-BINDING.
    9. "Structure of the photoreactive iron center of the nitrile hydratase from Rhodococcus sp. N-771. Evidence of a novel post-translational modification in the cysteine ligand."
      Tsujimura M., Dohmae N., Odaka M., Chijimatsu M., Takio K., Yohda M., Hoshino M., Nagashima S., Endo I.
      J. Biol. Chem. 272:29454-29459(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: EPR SPECTROSCOPY OF 106-129, IDENTIFICATION BY MASS SPECTROMETRY, OXIDATION AT CYS-113.
      Strain: N-771.

    Entry informationi

    Entry nameiNHAA_RHOER
    AccessioniPrimary (citable) accession number: P13448
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 106 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3