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Protein

Deaminated glutathione amidase

Gene

NIT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione.1 Publication

Catalytic activityi

N-(4-oxoglutarate)-L-cysteinylglycine + H2O = 2-oxoglutarate + L-cysteinylglycine.1 Publication

Kineticsi

kcat is 3.6 sec(-1) with dehydroglutathione.1 Publication
  1. KM=45 µM for dehydroglutathione at pH=8.51 Publication
  1. Vmax=5.8 µmol/min/mg enzyme with dehydroglutathione as substrate at pH=8.51 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei45Proton acceptorPROSITE-ProRule annotation1
Active sitei127Proton donorPROSITE-ProRule annotation1
Active sitei169NucleophilePROSITE-ProRule annotation1 Publication1
Binding sitei173Substrate1 Publication1
Binding sitei199Substrate1 Publication1

GO - Molecular functioni

  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: SGD

GO - Biological processi

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

BioCyciYEAST:YJL126W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Deaminated glutathione amidase1 Publication (EC:3.5.1.-1 Publication)
Short name:
dGSH amidase1 Publication
Alternative name(s):
Nitrilase homolog 1
Gene namesi
Name:NIT2
Ordered Locus Names:YJL126W
ORF Names:J0706
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL126W.
SGDiS000003662. NIT2.

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

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi169C → S: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002132551 – 307Deaminated glutathione amidaseAdd BLAST307

Proteomic databases

MaxQBiP47016.
PaxDbiP47016.
PRIDEiP47016.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi33630. 40 interactors.
STRINGi4932.YJL126W.

Structurei

Secondary structure

1307
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Helixi19 – 35Combined sources17
Beta strandi39 – 42Combined sources4
Helixi54 – 61Combined sources8
Helixi64 – 82Combined sources19
Beta strandi87 – 94Combined sources8
Helixi98 – 102Combined sources5
Beta strandi108 – 115Combined sources8
Beta strandi121 – 126Combined sources6
Beta strandi132 – 134Combined sources3
Beta strandi140 – 142Combined sources3
Helixi143 – 145Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi162 – 166Combined sources5
Helixi171 – 173Combined sources3
Helixi175 – 184Combined sources10
Beta strandi187 – 190Combined sources4
Helixi197 – 215Combined sources19
Beta strandi218 – 221Combined sources4
Beta strandi223 – 227Combined sources5
Helixi233 – 238Combined sources6
Turni243 – 246Combined sources4
Beta strandi251 – 253Combined sources3
Beta strandi257 – 259Combined sources3
Beta strandi265 – 268Combined sources4
Beta strandi277 – 284Combined sources8
Helixi285 – 294Combined sources10
Helixi297 – 299Combined sources3
Turni303 – 305Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4H5UX-ray1.92A/B/C/D1-307[»]
4HG3X-ray1.93A/B/C/D1-307[»]
4HG5X-ray1.91A/B/C/D1-307[»]
4HGDX-ray2.04A/B/C/D1-307[»]
ProteinModelPortaliP47016.
SMRiP47016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 285CN hydrolasePROSITE-ProRule annotationAdd BLAST280

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075099.
HOGENOMiHOG000222700.
InParanoidiP47016.
OMAiAAWVKGP.
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.

P47016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKLKRVAV AQLCSSADLT KNLKVVKELI SEAIQKKADV VFLPEASDYL
60 70 80 90 100
SQNPLHSRYL AQKSPKFIRQ LQSSITDLVR DNSRNIDVSI GVHLPPSEQD
110 120 130 140 150
LLEGNDRVRN VLLYIDHEGK ILQEYQKLHL FDVDVPNGPI LKESKSVQPG
160 170 180 190 200
KAIPDIIESP LGKLGSAICY DIRFPEFSLK LRSMGAEILC FPSAFTIKTG
210 220 230 240 250
EAHWELLGRA RAVDTQCYVL MPGQVGMHDL SDPEWEKQSH MSALEKSSRR
260 270 280 290 300
ESWGHSMVID PWGKIIAHAD PSTVGPQLIL ADLDRELLQE IRNKMPLWNQ

RRDDLFH
Length:307
Mass (Da):34,693
Last modified:February 1, 1996 - v1
Checksum:i48787C43B10A828E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284571 Genomic DNA. Translation: AAF87100.1.
Z49401 Genomic DNA. Translation: CAA89421.1.
BK006943 Genomic DNA. Translation: DAA08676.1.
PIRiS56907.
RefSeqiNP_012409.1. NM_001181559.1.

Genome annotation databases

EnsemblFungiiYJL126W; YJL126W; YJL126W.
GeneIDi853316.
KEGGisce:YJL126W.

Similar proteinsi

Entry informationi

Entry nameiNIT2_YEAST
AccessioniPrimary (citable) accession number: P47016
Secondary accession number(s): D6VW60, Q71SQ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 28, 2018
This is version 116 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