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Protein

Cobalt-containing nitrile hydratase subunit alpha

Gene
N/A
Organism
Pseudonocardia thermophila
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.Curated

Catalytic activityi

An aliphatic amide = a nitrile + H2O.Curated1 Publication

Cofactori

Co2+1 PublicationNote: Binds 1 Co2+ ion per heterodimer.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Cobalt
Metal bindingi111 – 1111Cobalt1 Publication
Metal bindingi112 – 1121Cobalt1 Publication
Metal bindingi113 – 1131Cobalt

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.84. 5208.

Names & Taxonomyi

Protein namesi
Recommended name:
Cobalt-containing nitrile hydratase subunit alpha (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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 204203Cobalt-containing nitrile hydratase subunit alphaPRO_0000186822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Cysteine sulfinic acid (-SO2H)1 Publication
Modified residuei113 – 1131Cysteine sulfenic acid (-SOH)1 Publication

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q7SID35EBI-1032292,EBI-1032285

Protein-protein interaction databases

IntActiQ7SID2. 1 interaction.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3021Combined sources
Helixi36 – 4813Combined sources
Helixi52 – 6413Combined sources
Helixi66 – 749Combined sources
Helixi76 – 816Combined sources
Turni82 – 843Combined sources
Beta strandi91 – 977Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi109 – 1113Combined sources
Helixi116 – 1194Combined sources
Helixi124 – 1274Combined sources
Helixi129 – 1357Combined sources
Helixi139 – 1479Combined sources
Beta strandi155 – 1617Combined sources
Beta strandi164 – 1718Combined sources
Helixi183 – 1875Combined sources
Helixi192 – 1965Combined sources
Beta strandi197 – 1993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IREX-ray1.80A1-204[»]
1UGPX-ray1.63A2-204[»]
1UGQX-ray2.00A2-204[»]
1UGRX-ray1.80A2-204[»]
1UGSX-ray2.00A2-204[»]
3VYHX-ray1.63A1-204[»]
4OB0X-ray1.20A1-204[»]
4OB1X-ray1.63A1-204[»]
4OB2X-ray1.52A2-204[»]
4OB3X-ray1.92A1-204[»]
ProteinModelPortaliQ7SID2.
SMRiQ7SID2. Positions 2-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SID2.

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.

Q7SID2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTENILRKSD EEIQKEITAR VKALESMLIE QGILTTSMID RMAEIYENEV
60 70 80 90 100
GPHLGAKVVV KAWTDPEFKK RLLADGTEAC KELGIGGLQG EDMMWVENTD
110 120 130 140 150
EVHHVVVCTL CSCYPWPVLG LPPNWFKEPQ YRSRVVREPR QLLKEEFGFE
160 170 180 190 200
VPPSKEIKVW DSSSEMRFVV LPQRPAGTDG WSEEELATLV TRESMIGVEP

AKAV
Length:204
Mass (Da):23,145
Last modified:January 23, 2007 - v3
Checksum:iBE390BBB7AEDD1BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111C → A (PubMed:11700034).Curated

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IREX-ray1.80A1-204[»]
1UGPX-ray1.63A2-204[»]
1UGQX-ray2.00A2-204[»]
1UGRX-ray1.80A2-204[»]
1UGSX-ray2.00A2-204[»]
3VYHX-ray1.63A1-204[»]
4OB0X-ray1.20A1-204[»]
4OB1X-ray1.63A1-204[»]
4OB2X-ray1.52A2-204[»]
4OB3X-ray1.92A1-204[»]
ProteinModelPortaliQ7SID2.
SMRiQ7SID2. Positions 2-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7SID2. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.2.1.84. 5208.

Miscellaneous databases

EvolutionaryTraceiQ7SID2.

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...

Publicationsi

  1. "Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia thermophila JCM3095."
    Yamaki T., Oikawa T., Ito K., Nakamura T.
    J. Ferment. Bioeng. 83:474-477(1997)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, CATALYTIC ACTIVITY, COFACTOR.
    Strain: ATCC 19285 / CBS 277.66 / DSM 43832 / JCM 3095 / NCIMB 10079.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), OXIDATION AT CYS-111 AND CYS-113.
    Strain: ATCC 19285 / CBS 277.66 / DSM 43832 / JCM 3095 / NCIMB 10079.

Entry informationi

Entry nameiNHAA_PSETH
AccessioniPrimary (citable) accession number: Q7SID2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 73 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.