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Protein

Nitrile hydratase subunit alpha

Gene

nthA

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
LigandIron, Metal-binding

Enzyme and pathway databases

SABIO-RKiP13448

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
IntActiP13448, 1 interactor

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
InterProiView protein in InterPro
IPR036648 CN_Hdrase_a/SCN_Hdrase_g_sf
IPR004232 CN_Hdrtase_a/SCN_Hdrlase_g
IPR023900 CN_Hdrtase_asu/SCN_Hdrlase_gsu
IPR018141 Nitrile_hydratase_asu
PfamiView protein in Pfam
PF02979 NHase_alpha, 1 hit
PIRSFiPIRSF001426 NHase_alpha, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD007559 CN_Hdrtase_asu/SCN_Hdrlase_gsu, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiNHAA_RHOER
AccessioniPrimary (citable) accession number: P13448
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 120 of the entry and version 3 of the sequence. See 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

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