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Protein

Nitrile hydratase subunit alpha

Gene

nthA

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed-Annotation score: 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 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)DescriptionActionsGraphical viewLength
Metal bindingi110Iron1
Metal bindingi113Iron1
Metal bindingi114Iron1
Metal bindingi115Iron1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001868232 – 207Nitrile hydratase subunit alphaAdd BLAST206

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei113Cysteine sulfinic acid (-SO2H)2 Publications1
Modified residuei115Cysteine sulfenic acid (-SOH)1 Publication1

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.
STRINGi234621.RER_59240.

Structurei

Secondary structure

1207
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 31Combined sources13
Turni32 – 34Combined sources3
Helixi40 – 50Combined sources11
Helixi54 – 66Combined sources13
Helixi68 – 76Combined sources9
Helixi78 – 84Combined sources7
Beta strandi92 – 99Combined sources8
Beta strandi104 – 109Combined sources6
Helixi118 – 121Combined sources4
Helixi126 – 129Combined sources4
Helixi131 – 136Combined sources6
Turni137 – 139Combined sources3
Helixi141 – 148Combined sources8
Beta strandi156 – 162Combined sources7
Beta strandi165 – 172Combined sources8
Helixi184 – 190Combined sources7
Helixi193 – 197Combined sources5
Beta strandi198 – 200Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3WVDX-ray1.18A1-207[»]
3WVEX-ray1.57A1-207[»]
3X20X-ray1.18A1-207[»]
3X24X-ray1.24A1-207[»]
3X25X-ray1.20A1-207[»]
3X26X-ray1.34A1-207[»]
3X28X-ray1.65A1-207[»]
ProteinModelPortaliP13448.
SMRiP13448.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13448.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EKJ. Bacteria.
ENOG410XR8T. LUCA.

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)DescriptionActionsGraphical viewLength
Sequence conflicti18P → A AA sequence (PubMed:2659343).Curated1
Sequence conflicti20S → T AA sequence (PubMed:2920826).Curated1

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.
PIRiB37806.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3WVDX-ray1.18A1-207[»]
3WVEX-ray1.57A1-207[»]
3X20X-ray1.18A1-207[»]
3X24X-ray1.24A1-207[»]
3X25X-ray1.20A1-207[»]
3X26X-ray1.34A1-207[»]
3X28X-ray1.65A1-207[»]
ProteinModelPortaliP13448.
SMRiP13448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6075N.
STRINGi234621.RER_59240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105EKJ. Bacteria.
ENOG410XR8T. LUCA.

Enzyme and pathway databases

SABIO-RKP13448.

Miscellaneous databases

EvolutionaryTraceiP13448.

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.
ProtoNetiSearch...

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 2, 2016
This is version 117 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.