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Protein

Glucosamine 6-phosphate N-acetyltransferase

Gene

GNA1

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

Catalytic activityi

Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate.1 Publication

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glucosamine 6-phosphate N-acetyltransferase (GNA1)
  2. Phosphoacetylglucosamine mutase (PCM1)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Substrate1 Publication
Binding sitei134 – 1341Substrate; via carbonyl oxygen1 Publication
Binding sitei158 – 1581Substrate1 Publication

GO - Molecular functioni

  • glucosamine 6-phosphate N-acetyltransferase activity Source: SGD

GO - Biological processi

  • UDP-N-acetylglucosamine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13174.
YEAST:YFL017C-MONOMER.
ReactomeiR-SCE-446210. Synthesis of UDP-N-acetyl-glucosamine.
SABIO-RKP43577.
UniPathwayiUPA00113; UER00529.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosamine 6-phosphate N-acetyltransferase (EC:2.3.1.41 Publication)
Alternative name(s):
Phosphoglucosamine acetylase
Phosphoglucosamine transacetylase
Gene namesi
Name:GNA1
Synonyms:PAT1
Ordered Locus Names:YFL017C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL017C.
SGDiS000001877. GNA1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 159158Glucosamine 6-phosphate N-acetyltransferasePRO_0000074552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP43577.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi31130. 52 interactions.
DIPiDIP-1349N.
IntActiP43577. 7 interactions.
MINTiMINT-411790.

Structurei

Secondary structure

1
159
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Beta strandi7 – 115Combined sources
Helixi14 – 163Combined sources
Helixi17 – 248Combined sources
Turni25 – 273Combined sources
Helixi35 – 4713Combined sources
Beta strandi60 – 623Combined sources
Beta strandi65 – 695Combined sources
Turni70 – 734Combined sources
Beta strandi74 – 8512Combined sources
Helixi88 – 914Combined sources
Beta strandi93 – 10210Combined sources
Helixi104 – 1063Combined sources
Helixi111 – 12515Combined sources
Beta strandi129 – 1357Combined sources
Helixi137 – 1393Combined sources
Helixi140 – 1456Combined sources
Beta strandi149 – 15810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I12X-ray1.30A/B/C/D1-159[»]
1I1DX-ray1.80A/B/C/D1-159[»]
1I21X-ray2.40A/B/M/N/X/Y1-159[»]
ProteinModelPortaliP43577.
SMRiP43577. Positions 1-159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43577.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 159132N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 894Substrate binding1 Publication
Regioni98 – 1003Substrate binding1 Publication
Regioni100 – 1023Acetyl-CoA bindingCombined sources1 Publication
Regioni108 – 1136Acetyl-CoA bindingCombined sources1 Publication
Regioni129 – 1302Substrate binding1 Publication
Regioni143 – 1453Acetyl-CoA bindingCombined sources1 Publication

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000008666.
HOGENOMiHOG000106325.
InParanoidiP43577.
KOiK00621.
OMAiGVEMQIR.
OrthoDBiEOG092C55DH.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLPDGFYIR RMEEGDLEQV TETLKVLTTV GTITPESFSK LIKYWNEATV
60 70 80 90 100
WNDNEDKKIM QYNPMVIVDK RTETVAATGN IIIERKIIHE LGLCGHIEDI
110 120 130 140 150
AVNSKYQGQG LGKLLIDQLV TIGFDYGCYK IILDCDEKNV KFYEKCGFSN

AGVEMQIRK
Length:159
Mass (Da):18,135
Last modified:November 1, 1995 - v1
Checksum:i2D2DD2D43A74C6F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 15948GKLLI…MQIRK → ASS in CAA86352 (Ref. 4) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017626 Genomic DNA. Translation: BAA36495.1.
D50617 Genomic DNA. Translation: BAA09221.1.
Z46255 Genomic DNA. Translation: CAA86352.1.
AY558564 Genomic DNA. Translation: AAS56890.1.
BK006940 Genomic DNA. Translation: DAA12423.1.
PIRiS56237.
RefSeqiNP_116637.1. NM_001179949.1.

Genome annotation databases

EnsemblFungiiBAA09221; BAA09221; BAA09221.
YFL017C; YFL017C; YFL017C.
GeneIDi850529.
KEGGisce:YFL017C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017626 Genomic DNA. Translation: BAA36495.1.
D50617 Genomic DNA. Translation: BAA09221.1.
Z46255 Genomic DNA. Translation: CAA86352.1.
AY558564 Genomic DNA. Translation: AAS56890.1.
BK006940 Genomic DNA. Translation: DAA12423.1.
PIRiS56237.
RefSeqiNP_116637.1. NM_001179949.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I12X-ray1.30A/B/C/D1-159[»]
1I1DX-ray1.80A/B/C/D1-159[»]
1I21X-ray2.40A/B/M/N/X/Y1-159[»]
ProteinModelPortaliP43577.
SMRiP43577. Positions 1-159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31130. 52 interactions.
DIPiDIP-1349N.
IntActiP43577. 7 interactions.
MINTiMINT-411790.

Proteomic databases

MaxQBiP43577.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09221; BAA09221; BAA09221.
YFL017C; YFL017C; YFL017C.
GeneIDi850529.
KEGGisce:YFL017C.

Organism-specific databases

EuPathDBiFungiDB:YFL017C.
SGDiS000001877. GNA1.

Phylogenomic databases

GeneTreeiENSGT00390000008666.
HOGENOMiHOG000106325.
InParanoidiP43577.
KOiK00621.
OMAiGVEMQIR.
OrthoDBiEOG092C55DH.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00529.
BioCyciMetaCyc:MONOMER-13174.
YEAST:YFL017C-MONOMER.
ReactomeiR-SCE-446210. Synthesis of UDP-N-acetyl-glucosamine.
SABIO-RKP43577.

Miscellaneous databases

EvolutionaryTraceiP43577.
PROiP43577.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGNA1_YEAST
AccessioniPrimary (citable) accession number: P43577
Secondary accession number(s): D6VTL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2550 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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