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Protein

Pyridoxal 5'-phosphate synthase subunit SNO1

Gene

SNO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform.Curated

Catalytic activityi

D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate.Curated
L-glutamine + H2O = L-glutamate + NH3.1 Publication

Kineticsi

  1. KM=3.4 mM for glutamine1 Publication
  1. Vmax=0.48 µmol/min/mg enzyme with glutamine as substrate1 Publication

Pathwayi: pyridoxal 5'-phosphate biosynthesis

This protein is involved in the pathway pyridoxal 5'-phosphate biosynthesis, which is part of Cofactor biosynthesis.Curated
View all proteins of this organism that are known to be involved in the pathway pyridoxal 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei100 – 1001NucleophileBy similarity
Binding sitei129 – 1291L-glutamineBy similarity
Active sitei203 – 2031Charge relay systemBy similarity
Active sitei205 – 2051Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutamine metabolic process Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: SGD
  • pyridoxal phosphate biosynthetic process Source: GO_Central
  • pyridoxine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32795-MONOMER.
YEAST:G3O-32795-MONOMER.
UniPathwayiUPA00245.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal 5'-phosphate synthase subunit SNO1 (EC:4.3.3.6)
Alternative name(s):
PDX2 homolog 1
Short name:
Pdx2.1
Pyridoxal 5'-phosphate synthase glutaminase subunit (EC:3.5.1.21 Publication)
Gene namesi
Name:SNO1
Ordered Locus Names:YMR095C
ORF Names:YM6543.02C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR095C.
SGDiS000004701. SNO1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • glutaminase complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Pyridoxal 5'-phosphate synthase subunit SNO1PRO_0000135619Add
BLAST

Proteomic databases

MaxQBiQ03144.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SNZ1Q031484EBI-28190,EBI-17618
SNZ2P538243EBI-28190,EBI-17623

Protein-protein interaction databases

BioGridi35270. 30 interactions.
DIPiDIP-1642N.
IntActiQ03144. 11 interactions.
MINTiMINT-386947.

Structurei

3D structure databases

ProteinModelPortaliQ03144.
SMRiQ03144. Positions 13-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 693L-glutamine bindingBy similarity
Regioni160 – 1612L-glutamine bindingBy similarity

Sequence similaritiesi

Belongs to the glutaminase PdxT/SNO family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

GeneTreeiENSGT00390000011516.
HOGENOMiHOG000039949.
InParanoidiQ03144.
KOiK08681.
OMAiRKASSHI.
OrthoDBiEOG7BW0W3.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR002161. PdxT/SNO.
IPR021196. PdxT/SNO_CS.
[Graphical view]
PfamiPF01174. SNO. 1 hit.
[Graphical view]
PIRSFiPIRSF005639. Glut_amidoT_SNO. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR03800. PLP_synth_Pdx2. 1 hit.
PROSITEiPS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03144-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKTHSTMSG KSMKVIGVLA LQGAFLEHTN HLKRCLAEND YGIKIEIKTV
60 70 80 90 100
KTPEDLAQCD ALIIPGGEST SMSLIAQRTG LYPCLYEFVH NPEKVVWGTC
110 120 130 140 150
AGLIFLSAQL ENESALVKTL GVLKVDVRRN AFGRQAQSFT QKCDFSNFIP
160 170 180 190 200
GCDNFPATFI RAPVIERILD PIAVKSLYEL PVNGKDVVVA ATQNHNILVT
210 220
SFHPELADSD TRFHDWFIRQ FVSN
Length:224
Mass (Da):24,907
Last modified:November 1, 1997 - v1
Checksum:iC0EC1B2382581D40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49807 Genomic DNA. Translation: CAA89896.1.
AY692745 Genomic DNA. Translation: AAT92764.1.
BK006946 Genomic DNA. Translation: DAA09992.1.
PIRiS55081.
RefSeqiNP_013813.1. NM_001182595.1.

Genome annotation databases

EnsemblFungiiYMR095C; YMR095C; YMR095C.
GeneIDi855120.
KEGGisce:YMR095C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49807 Genomic DNA. Translation: CAA89896.1.
AY692745 Genomic DNA. Translation: AAT92764.1.
BK006946 Genomic DNA. Translation: DAA09992.1.
PIRiS55081.
RefSeqiNP_013813.1. NM_001182595.1.

3D structure databases

ProteinModelPortaliQ03144.
SMRiQ03144. Positions 13-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35270. 30 interactions.
DIPiDIP-1642N.
IntActiQ03144. 11 interactions.
MINTiMINT-386947.

Proteomic databases

MaxQBiQ03144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR095C; YMR095C; YMR095C.
GeneIDi855120.
KEGGisce:YMR095C.

Organism-specific databases

EuPathDBiFungiDB:YMR095C.
SGDiS000004701. SNO1.

Phylogenomic databases

GeneTreeiENSGT00390000011516.
HOGENOMiHOG000039949.
InParanoidiQ03144.
KOiK08681.
OMAiRKASSHI.
OrthoDBiEOG7BW0W3.

Enzyme and pathway databases

UniPathwayiUPA00245.
BioCyciMetaCyc:G3O-32795-MONOMER.
YEAST:G3O-32795-MONOMER.

Miscellaneous databases

PROiQ03144.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR002161. PdxT/SNO.
IPR021196. PdxT/SNO_CS.
[Graphical view]
PfamiPF01174. SNO. 1 hit.
[Graphical view]
PIRSFiPIRSF005639. Glut_amidoT_SNO. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR03800. PLP_synth_Pdx2. 1 hit.
PROSITEiPS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Characterization of the products of the genes SNO1 and SNZ1 involved in pyridoxine synthesis in Saccharomyces cerevisiae."
    Dong Y.X., Sueda S., Nikawa J., Kondo H.
    Eur. J. Biochem. 271:745-752(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-9, FUNCTION AS GLUTAMINASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  5. Cited for: FUNCTION.

Entry informationi

Entry nameiSNO1_YEAST
AccessioniPrimary (citable) accession number: Q03144
Secondary accession number(s): D6VZR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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.