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Protein

Omega-amidase NIT3

Gene

NIT3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Miscellaneous

Present with 4510 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Kineticsi

kcat is 23.5 sec(-1) with 2-oxoglutaramate.1 Publication
  1. KM=1.6 mM for 2-oxoglutaramate at pH=8.51 Publication
  1. Vmax=40.2 µmol/min/mg enzyme with 2-oxoglutaramate as substrate at pH=8.51 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei53Proton acceptorPROSITE-ProRule annotation1
Active sitei128Proton donorPROSITE-ProRule annotation1
Active sitei169NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

BioCyciYEAST:YLR351C-MONOMER
ReactomeiR-SCE-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-amidase NIT31 Publication (EC:3.5.1.31 Publication)
Alternative name(s):
Nitrilase homolog 2
Gene namesi
Name:NIT3
Ordered Locus Names:YLR351C
ORF Names:L9638.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR351C
SGDiS000004343 NIT3

Subcellular locationi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002132561 – 291Omega-amidase NIT3Add BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49954
PaxDbiP49954
PRIDEiP49954

PTM databases

iPTMnetiP49954

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi31613, 30 interactors
DIPiDIP-4666N
IntActiP49954, 2 interactors
STRINGi4932.YLR351C

Structurei

Secondary structure

1291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi11 – 17Combined sources7
Helixi25 – 42Combined sources18
Beta strandi46 – 50Combined sources5
Turni53 – 56Combined sources4
Helixi61 – 67Combined sources7
Beta strandi73 – 75Combined sources3
Helixi78 – 89Combined sources12
Beta strandi93 – 95Combined sources3
Beta strandi99 – 102Combined sources4
Turni104 – 106Combined sources3
Beta strandi109 – 116Combined sources8
Beta strandi122 – 127Combined sources6
Helixi143 – 146Combined sources4
Beta strandi155 – 159Combined sources5
Beta strandi162 – 166Combined sources5
Helixi169 – 173Combined sources5
Helixi175 – 183Combined sources9
Beta strandi186 – 192Combined sources7
Helixi199 – 215Combined sources17
Beta strandi217 – 222Combined sources6
Beta strandi230 – 232Combined sources3
Beta strandi239 – 241Combined sources3
Beta strandi247 – 250Combined sources4
Beta strandi253 – 262Combined sources10
Helixi264 – 273Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F89X-ray2.40A/B1-291[»]
ProteinModelPortaliP49954
SMRiP49954
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49954

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 264CN hydrolasePROSITE-ProRule annotationAdd BLAST254

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074838
HOGENOMiHOG000222700
InParanoidiP49954
KOiK13566
OMAiTGKDHWQ
OrthoDBiEOG092C3EQE

Family and domain databases

Gene3Di3.60.110.10, 1 hit
InterProiView protein in InterPro
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
IPR001110 UPF0012_CS
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
SUPFAMiSSF56317 SSF56317, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit
PS01227 UPF0012, 1 hit

Sequencei

Sequence statusi: Complete.

P49954-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASKILSQK IKVALVQLSG SSPDKMANLQ RAATFIERAM KEQPDTKLVV
60 70 80 90 100
LPECFNSPYS TDQFRKYSEV INPKEPSTSV QFLSNLANKF KIILVGGTIP
110 120 130 140 150
ELDPKTDKIY NTSIIFNEDG KLIDKHRKVH LFDVDIPNGI SFHESETLSP
160 170 180 190 200
GEKSTTIDTK YGKFGVGICY DMRFPELAML SARKGAFAMI YPSAFNTVTG
210 220 230 240 250
PLHWHLLARS RAVDNQVYVM LCSPARNLQS SYHAYGHSIV VDPRGKIVAE
260 270 280 290
AGEGEEIIYA ELDPEVIESF RQAVPLTKQR RFDVYSDVNA H
Length:291
Mass (Da):32,549
Last modified:October 1, 1996 - v1
Checksum:iA813744120088827
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284572 Genomic DNA Translation: AAF87101.1
U19102 Genomic DNA Translation: AAB67751.1
BK006945 Genomic DNA Translation: DAA09655.1
PIRiS51459
RefSeqiNP_013455.1, NM_001182240.1

Genome annotation databases

EnsemblFungiiYLR351C; YLR351C; YLR351C
GeneIDi851065
KEGGisce:YLR351C

Similar proteinsi

Entry informationi

Entry nameiNIT3_YEAST
AccessioniPrimary (citable) accession number: P49954
Secondary accession number(s): D6VYY9, Q71SP9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health