Nitrile hydratase subunit alpha - Rhodococcus erythropolis

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P13448 (NHAA_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nitrile hydratase subunit alpha
Short name=NHase
Short name=Nitrilase
EC=4.2.1.84

Gene names

Name:

nthA

Organism

Rhodococcus erythropolis (Arthrobacter picolinophilus)

Taxonomic identifier

1833 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Ligand	Iron Metal-binding
Molecular function	Lyase
PTM	Oxidation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	indole-3-acetonitrile nitrile hydratase activity Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 207

206

Nitrile hydratase subunit alpha

PRO_0000186823

Sites

Metal binding

110

Iron

Metal binding

113

Iron

Metal binding

114

Iron

Metal binding

115

Iron

Amino acid modifications

Modified residue

113

Cysteine sulfinic acid (-SO2H)

Modified residue

115

Cysteine sulfenic acid (-SOH)

Experimental info

Sequence conflict

P → A AA sequence Ref.1

Sequence conflict

S → T AA sequence Ref.6

Secondary structure

207

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13448 [UniParc].

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

FASTA

207

22,996

        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), 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, 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.

PIR

B37806.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-206	[»]
2CZ0	X-ray	1.50	A	2-206	[»]
2CZ1	X-ray	1.39	A	2-206	[»]
2CZ6	X-ray	1.50	A	2-206	[»]
2CZ7	X-ray	1.80	A	2-206	[»]
2D0Q	X-ray	1.65	A	2-206	[»]
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	[»]

ProteinModelPortal

P13448.

SMR

P13448. Positions 10-207.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6075N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P13448.

Family and domain databases

Gene3D

3.90.330.10. 1 hit.

InterPro

IPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
IPR018141. Nitrile_hydratase_asu.
[Graphical view]

Pfam

PF02979. NHase_alpha. 1 hit.
[Graphical view]

PIRSF

PIRSF001426. NHase_alpha. 1 hit.

ProDom

PD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF56209. Nitrile_hydratase_asu. 1 hit.

TIGRFAMs

TIGR01323. nitrile_alph. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P13448.

Entry information

Entry name

NHAA_RHOER

Accession

Primary (citable) accession number: P13448

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents