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Protein

Omega-amidase NIT2

Gene

Nit2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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.2 Publications

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=0.0054 mM for alpha-ketoglutaramate (open-chain form)1 Publication
  1. Vmax=20.6 µmol/min/mg enzyme with alpha-ketoglutaramate as substrate1 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

ReactomeiR-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi1310494. Nit2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003202561 – 276Omega-amidase NIT2Add BLAST276

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26PhosphoserineBy similarity1
Modified residuei68N6-acetyllysine; alternateBy similarity1
Modified residuei68N6-succinyllysine; alternateBy similarity1
Modified residuei123N6-succinyllysineBy similarity1
Modified residuei130N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ497B0.
PRIDEiQ497B0.

PTM databases

iPTMnetiQ497B0.
PhosphoSitePlusiQ497B0.

Expressioni

Gene expression databases

BgeeiENSRNOG00000027797.
GenevisibleiQ497B0. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000034144.

Structurei

3D structure databases

ProteinModelPortaliQ497B0.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ497B0.
KOiK13566.
OMAiNPWGEVI.
OrthoDBiEOG091G0IKZ.
PhylomeDBiQ497B0.
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.

Q497B0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFRLALIQ LQVSSIKSDN ITRACSLVRE AAKQGANIVS LPECFNSPYG
60 70 80 90 100
TNYFPEYAEK IPGESTKKLS EVAKENSIYL IGGSIPEEDD GKLYNTCAVF
110 120 130 140 150
GPDGNLLVKH RKIHLFDIDV PGKITFQESK TLSPGDSFST FDTPYCRVGL
160 170 180 190 200
GICYDMRFAE LAQIYARRGC QLLVYPGAFN MTTGPAHWEL LQRARAVDNQ
210 220 230 240 250
VYVATASPAR DEKASYVAWG HSTVVDPWGQ VLTKAGTEET ILYSDIDLKK
260 270
LSEIRQQIPI LKQKRADLYS VESKKP
Length:276
Mass (Da):30,701
Last modified:September 13, 2005 - v1
Checksum:i38C64D674B171EF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC100637 mRNA. Translation: AAI00638.1.
RefSeqiNP_001029298.1. NM_001034126.1.
UniGeneiRn.42859.

Genome annotation databases

EnsembliENSRNOT00000029420; ENSRNOP00000034144; ENSRNOG00000027797.
GeneIDi288174.
KEGGirno:288174.
UCSCiRGD:1310494. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC100637 mRNA. Translation: AAI00638.1.
RefSeqiNP_001029298.1. NM_001034126.1.
UniGeneiRn.42859.

3D structure databases

ProteinModelPortaliQ497B0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000034144.

PTM databases

iPTMnetiQ497B0.
PhosphoSitePlusiQ497B0.

Proteomic databases

PaxDbiQ497B0.
PRIDEiQ497B0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000029420; ENSRNOP00000034144; ENSRNOG00000027797.
GeneIDi288174.
KEGGirno:288174.
UCSCiRGD:1310494. rat.

Organism-specific databases

CTDi56954.
RGDi1310494. Nit2.

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000074838.
HOGENOMiHOG000222700.
HOVERGENiHBG105126.
InParanoidiQ497B0.
KOiK13566.
OMAiNPWGEVI.
OrthoDBiEOG091G0IKZ.
PhylomeDBiQ497B0.
TreeFamiTF300747.

Enzyme and pathway databases

ReactomeiR-RNO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiQ497B0.

Gene expression databases

BgeeiENSRNOG00000027797.
GenevisibleiQ497B0. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q497B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 13, 2005
Last modified: November 30, 2016
This is version 73 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

Complete proteome, Reference proteome

Documents

  1. 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.