Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Omega-amidase NIT2

Gene

Nit2

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

Functioni

Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively.1 Publication

Catalytic activityi

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

Kineticsi

In solution, 2-oxoglutaramate 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 (PubMed:19596042). kcat is 10.7 sec(-1) with 2-oxoglutaramate (PubMed:28373563).2 Publications
  1. KM=0.195 mM for 2-oxoglutaramate at pH=8.51 Publication
  2. KM=0.25 mM for 2-oxoglutaramate at pH=8.51 Publication
  3. KM=1.27 mM for glutaramate at pH=8.51 Publication
  4. KM=0.14 mM for succinamate at pH=8.51 Publication
  5. KM=0.017 mM for 2-oxosuccinamate at pH=8.51 Publication
  6. KM=0.012 mM for 2-oxosuccinamate at pH=7.21 Publication
  7. KM=1.48 mM for gamma-monomethyl-alpha-ketoglutarate at pH=7.21 Publication
  8. KM=1.27 mM for glutaramate at pH=7.21 Publication
  9. KM=0.14 mM for glutaramate at pH=7.21 Publication
  1. Vmax=32.0 µmol/min/mg enzyme with 2-oxoglutaramate as substrate at pH=8.51 Publication
  2. Vmax=19.4 µmol/min/mg enzyme with 2-oxoglutaramate as substrate at pH=8.51 Publication
  3. Vmax=1.6 µmol/min/mg enzyme with 2-oxosuccinamate as substrate at pH=8.51 Publication
  4. Vmax=16 µmol/min/mg enzyme with glutaramate as substrate at pH=8.51 Publication
  5. Vmax=5.1 µmol/min/mg enzyme with glutaramate as substrate at pH=8.51 Publication
  6. Vmax=245.2 µmol/min/mg enzyme with gamma-monomethyl-alpha-ketoglutarate as substrate at pH=7.21 Publication
  7. Vmax=7.5 µmol/min/mg enzyme with glutaramate as substrate at pH=7.21 Publication
  8. Vmax=3.6 µmol/min/mg enzyme with glutaramate as substrate at pH=7.21 Publication
  9. Vmax=2.1 µmol/min/mg enzyme with 2-oxosuccinamate 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

Keywordsi

Molecular functionHydrolase

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1261838 Nit2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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-2DPAGEiIPI00119945

PTM databases

iPTMnetiQ9JHW2
PhosphoSitePlusiQ9JHW2
SwissPalmiQ9JHW2

Expressioni

Gene expression databases

BgeeiENSMUSG00000022751 Expressed in 249 organ(s), highest expression level in liver
CleanExiMM_NIT2
GenevisibleiQ9JHW2 MM

Interactioni

Subunit structurei

May form dimer.1 Publication

Protein-protein interaction databases

IntActiQ9JHW2, 3 interactors
MINTiQ9JHW2
STRINGi10090.ENSMUSP00000023432

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9JHW2
SMRiQ9JHW2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHW2

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 248CN hydrolasePROSITE-ProRule annotationAdd BLAST245

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

Gene3Di3.60.110.10, 1 hit
InterProiView protein in InterPro
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
SUPFAMiSSF56317 SSF56317, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A338P6G0A0A338P6G0_MOUSE
Omega-amidase NIT2
Nit2
196Annotation score:
A0A338P6Z4A0A338P6Z4_MOUSE
Omega-amidase NIT2
Nit2
69Annotation score:
A0A338P7A1A0A338P7A1_MOUSE
Omega-amidase NIT2
Nit2
148Annotation score:

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

Similar proteinsi

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
MINTiQ9JHW2
STRINGi10090.ENSMUSP00000023432

PTM databases

iPTMnetiQ9JHW2
PhosphoSitePlusiQ9JHW2
SwissPalmiQ9JHW2

2D gel databases

REPRODUCTION-2DPAGEiIPI00119945

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
OMAiTGKDHWQ
OrthoDBiEOG091G0IKZ
PhylomeDBiQ9JHW2
TreeFamiTF300747

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9JHW2
PROiPR:Q9JHW2
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022751 Expressed in 249 organ(s), highest expression level in liver
CleanExiMM_NIT2
GenevisibleiQ9JHW2 MM

Family and domain databases

Gene3Di3.60.110.10, 1 hit
InterProiView protein in InterPro
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
SUPFAMiSSF56317 SSF56317, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNIT2_MOUSE
AccessioniPrimary (citable) accession number: Q9JHW2
Secondary accession number(s): Q9CTG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: September 12, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again