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P13449 (NHAB_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 beta
Short name=NHase
Short name=Nitrilase
EC=4.2.1.84
Gene names
Name:nthB
Synonyms:nha2
OrganismRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifier1833 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

An aliphatic amide = a nitrile + H2O.

Subunit structure

Heterodimer of an alpha and a beta chain.

Biotechnological use

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

Sequence similarities

Belongs to the nitrile hydratase subunit beta family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Nitrile hydratase subunit beta
PRO_0000186831

Natural variations

Natural variant401M → V in strain: ACV2.

Secondary structure

1 ............................ 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13449 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: A0401CA4FC1C2CBE

FASTA21223,487
        10         20         30         40         50         60 
MDGVHDLAGV QGFGKVPHTV NADIGPTFHA EWEHLPYSLM FAGVAELGAF SVDEVRYVVE 

        70         80         90        100        110        120 
RMEPRHYMMT PYYERYVIGV ATLMVEKGIL TQDELESLAG GPFPLSRPSE SEGRPAPVET 

       130        140        150        160        170        180 
TTFEVGQRVR VRDEYVPGHI RMPAYCRGRV GTISHRTTEK WPFPDAIGHG RNDAGEEPTY 

       190        200        210 
HVKFAAEELF GSDTDGGSVV VDLFEGYLEP AA

« 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]"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), MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP13449.
SMRP13449. Positions 1-212.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6076N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP13449.

Family and domain databases

InterProIPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
IPR003168. Nitrile_hydratase_bsu.
[Graphical view]
PfamPF02211. NHase_beta. 1 hit.
[Graphical view]
PIRSFPIRSF001427. NHase_beta. 1 hit.
SUPFAMSSF50090. E_transp_acc. 1 hit.
TIGRFAMsTIGR03888. nitrile_beta. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP13449.

Entry information

Entry nameNHAB_RHOER
AccessionPrimary (citable) accession number: P13449
Secondary accession number(s): Q59789
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents