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Protein

Cobalt-containing nitrile hydratase subunit beta

Gene
N/A
Organism
Pseudonocardia thermophila
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

An aliphatic amide = a nitrile + H2O.Curated1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Names & Taxonomyi

Protein namesi
Recommended name:
Cobalt-containing nitrile hydratase subunit beta (EC:4.2.1.84)
Short name:
L-NHase
Short name:
L-nitrilase
OrganismiPseudonocardia thermophilaImported
Taxonomic identifieri1848 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaePseudonocardia

Pathology & Biotechi

Biotechnological usei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001868301 – 233Cobalt-containing nitrile hydratase subunit betaAdd BLAST233

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q7SID25EBI-1032285,EBI-1032292

Protein-protein interaction databases

IntActiQ7SID3. 1 interactor.

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 42Combined sources15
Helixi48 – 56Combined sources9
Helixi60 – 65Combined sources6
Helixi68 – 82Combined sources15
Helixi88 – 100Combined sources13
Helixi113 – 125Combined sources13
Beta strandi144 – 147Combined sources4
Helixi160 – 162Combined sources3
Beta strandi166 – 176Combined sources11
Helixi179 – 182Combined sources4
Turni183 – 185Combined sources3
Beta strandi191 – 199Combined sources9
Helixi200 – 204Combined sources5
Helixi205 – 207Combined sources3
Beta strandi212 – 219Combined sources8
Helixi220 – 222Combined sources3
Beta strandi223 – 227Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IREX-ray1.80B1-228[»]
1UGPX-ray1.63B1-226[»]
1UGQX-ray2.00B1-228[»]
1UGRX-ray1.80B1-228[»]
1UGSX-ray2.00B1-228[»]
3VYHX-ray1.63B1-233[»]
4OB0X-ray1.20B1-233[»]
4OB1X-ray1.63B1-233[»]
4OB2X-ray1.52B1-233[»]
4OB3X-ray1.92B1-233[»]
ProteinModelPortaliQ7SID3.
SMRiQ7SID3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SID3.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
IPR003168. Nitrile_hydratase_bsu.
[Graphical view]
PfamiPF02211. NHase_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF001427. NHase_beta. 1 hit.
SUPFAMiSSF50090. SSF50090. 1 hit.
TIGRFAMsiTIGR03888. nitrile_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7SID3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGVYDVGGT DGLGPINRPA DEPVFRAEWE KVAFAMFPAT FRAGFMGLDE
60 70 80 90 100
FRFGIEQMNP AEYLESPYYW HWIRTYIHHG VRTGKIDLEE LERRTQYYRE
110 120 130 140 150
NPDAPLPEHE QKPELIEFVN QAVYGGLPAS REVDRPPKFK EGDVVRFSTA
160 170 180 190 200
SPKGHARRAR YVRGKTGTVV KHHGAYIYPD TAGNGLGECP EHLYTVRFTA
210 220 230
QELWGPEGDP NSSVYYDCWE PYIELVDTKA AAA
Length:233
Mass (Da):26,550
Last modified:March 1, 2004 - v2
Checksum:iECA070F18BCE62F0
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IREX-ray1.80B1-228[»]
1UGPX-ray1.63B1-226[»]
1UGQX-ray2.00B1-228[»]
1UGRX-ray1.80B1-228[»]
1UGSX-ray2.00B1-228[»]
3VYHX-ray1.63B1-233[»]
4OB0X-ray1.20B1-233[»]
4OB1X-ray1.63B1-233[»]
4OB2X-ray1.52B1-233[»]
4OB3X-ray1.92B1-233[»]
ProteinModelPortaliQ7SID3.
SMRiQ7SID3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7SID3. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SID3.

Family and domain databases

InterProiIPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
IPR003168. Nitrile_hydratase_bsu.
[Graphical view]
PfamiPF02211. NHase_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF001427. NHase_beta. 1 hit.
SUPFAMiSSF50090. SSF50090. 1 hit.
TIGRFAMsiTIGR03888. nitrile_beta. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNHAB_PSETH
AccessioniPrimary (citable) accession number: Q7SID3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: November 2, 2016
This is version 66 of the entry and version 2 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.