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Protein

Glucosamine 6-phosphate N-acetyltransferase

Gene

gna-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate.By similarity

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 (gna-1)
  2. no protein annotated in this organism
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 sitei44 – 441SubstrateBy similarity
Binding sitei164 – 1641SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-CEL-446210. Synthesis of UDP-N-acetyl-glucosamine.
UniPathwayiUPA00113; UER00529.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosamine 6-phosphate N-acetyltransferase (EC:2.3.1.4By similarity)
Alternative name(s):
Phosphoglucosamine acetylase
Phosphoglucosamine transacetylase
Gene namesi
Name:gna-1
ORF Names:B0024.12
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiB0024.12; CE05156; WBGene00001646; gna-1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Glucosamine 6-phosphate N-acetyltransferasePRO_0000074556Add
BLAST

Proteomic databases

EPDiQ17427.
PaxDbiQ17427.
PRIDEiQ17427.

Interactioni

Protein-protein interaction databases

BioGridi44467. 4 interactions.
DIPiDIP-25958N.
IntActiQ17427. 4 interactions.
MINTiMINT-1068708.
STRINGi6239.B0024.12.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi7 – 104Combined sources
Helixi11 – 133Combined sources
Beta strandi22 – 265Combined sources
Helixi29 – 324Combined sources
Turni33 – 353Combined sources
Helixi36 – 438Combined sources
Helixi51 – 6212Combined sources
Beta strandi69 – 757Combined sources
Turni76 – 783Combined sources
Beta strandi81 – 9111Combined sources
Helixi94 – 974Combined sources
Beta strandi99 – 10810Combined sources
Helixi110 – 1123Combined sources
Helixi117 – 13216Combined sources
Beta strandi135 – 1395Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 1505Combined sources
Turni151 – 1533Combined sources
Beta strandi161 – 1633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AG7X-ray1.55A/B1-165[»]
4AG9X-ray1.76A/B1-165[»]
ProteinModelPortaliQ17427.
SMRiQ17427. Positions 1-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 165144N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni92 – 954Substrate bindingBy similarity
Regioni104 – 1063Substrate bindingBy similarity
Regioni114 – 1196Acetyl-CoA bindingBy similarity
Regioni135 – 1362Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3396. Eukaryota.
COG0454. LUCA.
GeneTreeiENSGT00390000008666.
HOGENOMiHOG000106325.
InParanoidiQ17427.
KOiK00621.
OMAiKFIHNCA.
OrthoDBiEOG77T165.
PhylomeDBiQ17427.

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.

Q17427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHIFDASVL APHIPSNLPD NFKVRPLAKD DFSKGYVDLL SQLTSVGNLD
60 70 80 90 100
QEAFEKRFEA MRTSVPNYHI VVIEDSNSQK VVASASLVVE MKFIHGAGSR
110 120 130 140 150
GRVEDVVVDT EMRRQKLGAV LLKTLVSLGK SLGVYKISLE CVPELLPFYS
160
QFGFQDDCNF MTQRF
Length:165
Mass (Da):18,459
Last modified:November 1, 1996 - v1
Checksum:i215C7CD7A6165BB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017628 mRNA. Translation: BAA36497.1.
Z71178 Genomic DNA. Translation: CAA94884.1.
PIRiT37319.
RefSeqiNP_505654.1. NM_073253.5.
UniGeneiCel.19593.

Genome annotation databases

EnsemblMetazoaiB0024.12; B0024.12; WBGene00001646.
GeneIDi179437.
KEGGicel:CELE_B0024.12.
UCSCiB0024.12. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017628 mRNA. Translation: BAA36497.1.
Z71178 Genomic DNA. Translation: CAA94884.1.
PIRiT37319.
RefSeqiNP_505654.1. NM_073253.5.
UniGeneiCel.19593.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AG7X-ray1.55A/B1-165[»]
4AG9X-ray1.76A/B1-165[»]
ProteinModelPortaliQ17427.
SMRiQ17427. Positions 1-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44467. 4 interactions.
DIPiDIP-25958N.
IntActiQ17427. 4 interactions.
MINTiMINT-1068708.
STRINGi6239.B0024.12.

Proteomic databases

EPDiQ17427.
PaxDbiQ17427.
PRIDEiQ17427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiB0024.12; B0024.12; WBGene00001646.
GeneIDi179437.
KEGGicel:CELE_B0024.12.
UCSCiB0024.12. c. elegans.

Organism-specific databases

CTDi179437.
WormBaseiB0024.12; CE05156; WBGene00001646; gna-1.

Phylogenomic databases

eggNOGiKOG3396. Eukaryota.
COG0454. LUCA.
GeneTreeiENSGT00390000008666.
HOGENOMiHOG000106325.
InParanoidiQ17427.
KOiK00621.
OMAiKFIHNCA.
OrthoDBiEOG77T165.
PhylomeDBiQ17427.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00529.
ReactomeiR-CEL-446210. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

NextBioi905386.
PROiQ17427.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis."
    Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.
    J. Biol. Chem. 274:424-429(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiGNA1_CAEEL
AccessioniPrimary (citable) accession number: Q17427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.