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P13448

- NHAA_RHOER

UniProt

P13448 - NHAA_RHOER

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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

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

Fe3+Note: Binds 1 Fe(3+) 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
Complete GO annotation...

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 – 3113Combined sources
Turni32 – 343Combined sources
Helixi40 – 5011Combined sources
Helixi54 – 6613Combined sources
Helixi68 – 769Combined sources
Helixi78 – 847Combined sources
Beta strandi92 – 998Combined sources
Beta strandi104 – 1096Combined sources
Helixi118 – 1214Combined sources
Helixi126 – 1294Combined sources
Helixi131 – 1366Combined sources
Turni137 – 1393Combined sources
Helixi141 – 1488Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi165 – 1728Combined sources
Helixi184 – 1907Combined sources
Helixi193 – 1975Combined sources
Beta strandi198 – 2003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSVTIDHTTE NAAPAQAPVS DRAWALFRAL DGKGLVPDGY VEGWKKTFEE
60 70 80 90 100
DFSPRRGAEL VARAWTDPEF RQLLLTDGTA AVAQYGYLGP QGEYIVAVED
110 120 130 140 150
TPTLKNVIVC SLCSCTAWPI LGLPPTWYKS FEYRARVVRE PRKVLSEMGT
160 170 180 190 200
EIASDIEIRV YDTTAETRYM VLPQRPAGTE GWSQEQLQEI VTKDCLIGVA

IPQVPTV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 107 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