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P13448 (NHAA_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrile hydratase subunit alpha

Short name=NHase
Short name=Nitrilase
EC=4.2.1.84
Gene names
Name:nthA
OrganismRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifier1833 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

An aliphatic amide = a nitrile + H2O.

Cofactor

Binds 1 Fe3+ ion per subunit.

Enzyme regulation

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.

Subunit structure

Heterodimer of an alpha and a beta chain.

Post-translational modification

Oxidation on Cys-113 is essential for the activity.

Oxidation on Cys-115 stabilizes the Fe-NO ligand coordinated in the inactive form.

Sequence similarities

Belongs to the nitrile hydratase subunit alpha family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 207206Nitrile hydratase subunit alpha
PRO_0000186823

Sites

Metal binding1101Iron
Metal binding1131Iron
Metal binding1141Iron
Metal binding1151Iron

Amino acid modifications

Modified residue1131Cysteine sulfinic acid (-SO2H)
Modified residue1151Cysteine sulfenic acid (-SOH)

Experimental info

Sequence conflict181P → A AA sequence Ref.1
Sequence conflict201S → T AA sequence Ref.6

Secondary structure

.................................. 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13448 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 22DD21260A2D70E5

FASTA20722,996
        10         20         30         40         50         60 
MSVTIDHTTE NAAPAQAPVS DRAWALFRAL DGKGLVPDGY VEGWKKTFEE DFSPRRGAEL 

        70         80         90        100        110        120 
VARAWTDPEF RQLLLTDGTA AVAQYGYLGP QGEYIVAVED TPTLKNVIVC SLCSCTAWPI 

       130        140        150        160        170        180 
LGLPPTWYKS FEYRARVVRE PRKVLSEMGT EIASDIEIRV YDTTAETRYM VLPQRPAGTE 

       190        200 
GWSQEQLQEI VTKDCLIGVA IPQVPTV 

« Hide

References

[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, 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB37806.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP13448.
SMRP13448. Positions 10-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6075N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP13448.

Family and domain databases

Gene3D3.90.330.10. 1 hit.
InterProIPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
IPR018141. Nitrile_hydratase_asu.
[Graphical view]
PfamPF02979. NHase_alpha. 1 hit.
[Graphical view]
PIRSFPIRSF001426. NHase_alpha. 1 hit.
ProDomPD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56209. SSF56209. 1 hit.
TIGRFAMsTIGR01323. nitrile_alph. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP13448.

Entry information

Entry nameNHAA_RHOER
AccessionPrimary (citable) accession number: P13448
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references