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Protein

Omega-amidase NIT2

Gene

Nit2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively.1 Publication

Catalytic activityi

A monoamide of a dicarboxylate + H2O = a dicarboxylate + NH3.1 Publication

Kineticsi

In solution, alpha-ketoglutaramate is in equilibrium with a cyclic form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of ring opening is no longer limiting for the omega-amidase reaction.

  1. KM=0.195 mM for alpha-ketoglutaramate at pH=8.51 Publication
  2. KM=1.27 mM for glutaramate at pH=8.51 Publication
  3. KM=0.14 mM for succinamate at pH=8.51 Publication
  4. KM=0.017 mM for alpha-ketosuccinamate at pH=8.51 Publication
  5. KM=0.012 mM for alpha-ketosuccinamate at pH=7.21 Publication
  6. KM=1.48 mM for gamma-monomethyl-alpha-ketoglutarate at pH=7.21 Publication
  7. KM=1.27 mM for glutaramate at pH=7.21 Publication
  8. KM=0.14 mM for glutaramate at pH=7.21 Publication
  1. Vmax=32.0 µmol/min/mg enzyme with alpha-ketoglutaramate as substrate at pH=8.51 Publication
  2. Vmax=1.6 µmol/min/mg enzyme with alpha-ketosuccinamate as substrate at pH=8.51 Publication
  3. Vmax=16 µmol/min/mg enzyme with glutaramate as substrate at pH=8.51 Publication
  4. Vmax=5.1 µmol/min/mg enzyme with glutaramate as substrate at pH=8.51 Publication
  5. Vmax=245.2 µmol/min/mg enzyme with gamma-monomethyl-alpha-ketoglutarate as substrate at pH=7.21 Publication
  6. Vmax=7.5 µmol/min/mg enzyme with glutaramate as substrate at pH=7.21 Publication
  7. Vmax=3.6 µmol/min/mg enzyme with glutaramate as substrate at pH=7.21 Publication
  8. Vmax=2.1 µmol/min/mg enzyme with alpha-ketosuccinamate as substrate at pH=7.21 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei43Proton acceptorPROSITE-ProRule annotation1
Active sitei112Proton donorPROSITE-ProRule annotation1
Active sitei153NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18738.
ReactomeiR-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-amidase NIT2 (EC:3.5.1.31 Publication)
Alternative name(s):
Nitrilase homolog 2
Gene namesi
Name:Nit2
Synonyms:D16Ertd502e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1261838. Nit2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003202541 – 276Omega-amidase NIT2Add BLAST276

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26PhosphoserineBy similarity1
Modified residuei68N6-acetyllysine; alternateCombined sources1
Modified residuei68N6-succinyllysine; alternateCombined sources1
Modified residuei123N6-succinyllysineCombined sources1
Modified residuei130N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JHW2.
MaxQBiQ9JHW2.
PaxDbiQ9JHW2.
PeptideAtlasiQ9JHW2.
PRIDEiQ9JHW2.

2D gel databases

REPRODUCTION-2DPAGEIPI00119945.

PTM databases

iPTMnetiQ9JHW2.
PhosphoSitePlusiQ9JHW2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022751.
CleanExiMM_NIT2.
GenevisibleiQ9JHW2. MM.

Interactioni

Subunit structurei

May form dimer.1 Publication

Protein-protein interaction databases

IntActiQ9JHW2. 3 interactors.
MINTiMINT-4129730.
STRINGi10090.ENSMUSP00000023432.

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Helixi17 – 33Combined sources17
Beta strandi37 – 40Combined sources4
Turni43 – 46Combined sources4
Turni51 – 53Combined sources3
Helixi54 – 57Combined sources4
Beta strandi61 – 63Combined sources3
Helixi64 – 76Combined sources13
Beta strandi78 – 81Combined sources4
Beta strandi85 – 89Combined sources5
Beta strandi92 – 100Combined sources9
Beta strandi106 – 111Combined sources6
Beta strandi117 – 120Combined sources4
Turni121 – 123Combined sources3
Beta strandi124 – 127Combined sources4
Helixi128 – 130Combined sources3
Beta strandi140 – 142Combined sources3
Beta strandi147 – 150Combined sources4
Helixi153 – 157Combined sources5
Helixi159 – 167Combined sources9
Beta strandi170 – 176Combined sources7
Helixi183 – 199Combined sources17
Beta strandi202 – 206Combined sources5
Beta strandi214 – 216Combined sources3
Beta strandi223 – 225Combined sources3
Beta strandi231 – 234Combined sources4
Beta strandi237 – 247Combined sources11
Helixi248 – 257Combined sources10
Helixi260 – 262Combined sources3
Turni266 – 268Combined sources3
Beta strandi269 – 273Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W1VX-ray1.49A/B1-276[»]
ProteinModelPortaliQ9JHW2.
SMRiQ9JHW2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHW2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 270CN hydrolasePROSITE-ProRule annotationAdd BLAST267

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000074838.
HOGENOMiHOG000222700.
HOVERGENiHBG105126.
InParanoidiQ9JHW2.
KOiK13566.
OMAiNPWGEVI.
OrthoDBiEOG091G0IKZ.
PhylomeDBiQ9JHW2.
TreeFamiTF300747.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFRLALIQ LQVSSIKSDN LTRACSLVRE AAKQGANIVS LPECFNSPYG
60 70 80 90 100
TTYFPDYAEK IPGESTQKLS EVAKESSIYL IGGSIPEEDA GKLYNTCSVF
110 120 130 140 150
GPDGSLLVKH RKIHLFDIDV PGKITFQESK TLSPGDSFST FDTPYCKVGL
160 170 180 190 200
GICYDMRFAE LAQIYAQRGC QLLVYPGAFN LTTGPAHWEL LQRARAVDNQ
210 220 230 240 250
VYVATASPAR DDKASYVAWG HSTVVDPWGQ VLTKAGTEET ILYSDIDLKK
260 270
LAEIRQQIPI LKQKRADLYT VESKKP
Length:276
Mass (Da):30,502
Last modified:October 1, 2000 - v1
Checksum:i740FDC44978326D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284573 mRNA. Translation: AAF87102.1.
AK003604 mRNA. Translation: BAB22884.1.
AK004535 mRNA. Translation: BAB23354.1.
BC020153 mRNA. Translation: AAH20153.1.
CCDSiCCDS37363.1.
RefSeqiNP_075664.1. NM_023175.1.
UniGeneiMm.383203.

Genome annotation databases

EnsembliENSMUST00000023432; ENSMUSP00000023432; ENSMUSG00000022751.
GeneIDi52633.
KEGGimmu:52633.
UCSCiuc007zna.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284573 mRNA. Translation: AAF87102.1.
AK003604 mRNA. Translation: BAB22884.1.
AK004535 mRNA. Translation: BAB23354.1.
BC020153 mRNA. Translation: AAH20153.1.
CCDSiCCDS37363.1.
RefSeqiNP_075664.1. NM_023175.1.
UniGeneiMm.383203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W1VX-ray1.49A/B1-276[»]
ProteinModelPortaliQ9JHW2.
SMRiQ9JHW2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHW2. 3 interactors.
MINTiMINT-4129730.
STRINGi10090.ENSMUSP00000023432.

PTM databases

iPTMnetiQ9JHW2.
PhosphoSitePlusiQ9JHW2.

2D gel databases

REPRODUCTION-2DPAGEIPI00119945.

Proteomic databases

EPDiQ9JHW2.
MaxQBiQ9JHW2.
PaxDbiQ9JHW2.
PeptideAtlasiQ9JHW2.
PRIDEiQ9JHW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023432; ENSMUSP00000023432; ENSMUSG00000022751.
GeneIDi52633.
KEGGimmu:52633.
UCSCiuc007zna.1. mouse.

Organism-specific databases

CTDi56954.
MGIiMGI:1261838. Nit2.

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000074838.
HOGENOMiHOG000222700.
HOVERGENiHBG105126.
InParanoidiQ9JHW2.
KOiK13566.
OMAiNPWGEVI.
OrthoDBiEOG091G0IKZ.
PhylomeDBiQ9JHW2.
TreeFamiTF300747.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18738.
ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiQ9JHW2.
PROiQ9JHW2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022751.
CleanExiMM_NIT2.
GenevisibleiQ9JHW2. MM.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNIT2_MOUSE
AccessioniPrimary (citable) accession number: Q9JHW2
Secondary accession number(s): Q9CTG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.