GNA1_ORYSJ
ID GNA1_ORYSJ Reviewed; 165 AA.
AC Q5U9F2; A0A0N7KR10;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase 1;
DE EC=2.3.1.4 {ECO:0000269|PubMed:15849305};
DE AltName: Full=Glucose-6-phosphate acetyltransferase 1;
DE Short=OsGNA1;
DE AltName: Full=Phosphoglucosamine acetylase 1;
DE AltName: Full=Phosphoglucosamine transacetylase 1;
GN Name=GNA1; OrderedLocusNames=Os09g0488000, LOC_Os09g31310;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15849305; DOI=10.1104/pp.104.058248;
RA Jiang H., Wang S., Dang L., Wang S., Chen H., Wu Y., Jiang X., Wu P.;
RT "A novel short-root gene encodes a glucosamine-6-phosphate
RT acetyltransferase required for maintaining normal root cell shape in
RT rice.";
RL Plant Physiol. 138:232-242(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Acetyltransferase involved in de novo biosynthesis of UDP-N-
CC acetylglucosamine (UDP-GlcNAc) in roots and is required for maintaining
CC normal root cell shape. UDP-GlcNAc is an essential metabolite that
CC serves as an initial sugar donor for N-glycan synthesis and thus plays
CC an important role in protein and lipid glycosylation.
CC {ECO:0000269|PubMed:15849305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-
CC acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4;
CC Evidence={ECO:0000269|PubMed:15849305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for acetyl-coenzyme A {ECO:0000269|PubMed:15849305};
CC KM=145 uM for glucosamine-6-phosphate {ECO:0000269|PubMed:15849305};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the root elongation zone and at
CC lower levels in leaves and grains. {ECO:0000269|PubMed:15849305}.
CC -!- DISRUPTION PHENOTYPE: Short roots, disruption of microtubules and
CC shrinkage of cells in the root elongation zone.
CC {ECO:0000269|PubMed:15849305}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY772189; AAV40998.1; -; mRNA.
DR EMBL; AC108758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008215; BAF25444.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08714.1; -; Genomic_DNA.
DR EMBL; AK063214; BAG88597.1; -; mRNA.
DR RefSeq; XP_015610795.1; XM_015755309.1.
DR AlphaFoldDB; Q5U9F2; -.
DR SMR; Q5U9F2; -.
DR STRING; 4530.OS09T0488000-01; -.
DR PaxDb; Q5U9F2; -.
DR PRIDE; Q5U9F2; -.
DR EnsemblPlants; Os09t0488000-01; Os09t0488000-01; Os09g0488000.
DR GeneID; 4347432; -.
DR Gramene; Os09t0488000-01; Os09t0488000-01; Os09g0488000.
DR KEGG; osa:4347432; -.
DR eggNOG; KOG3396; Eukaryota.
DR HOGENOM; CLU_072095_3_0_1; -.
DR InParanoid; Q5U9F2; -.
DR OMA; RGRGCYK; -.
DR OrthoDB; 1479446at2759; -.
DR PlantReactome; R-OSA-1119386; UDP-N-acetylgalactosamine biosynthesis.
DR PlantReactome; R-OSA-9030654; Primary root development.
DR SABIO-RK; Q5U9F2; -.
DR UniPathway; UPA00113; UER00529.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q5U9F2; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006045; P:N-acetylglucosamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039143; GNPNAT1.
DR PANTHER; PTHR13355; PTHR13355; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase.
FT CHAIN 1..165
FT /note="Glucosamine 6-phosphate N-acetyltransferase 1"
FT /id="PRO_0000421038"
FT DOMAIN 22..165
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 114..119
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 135..136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 149..151
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
SQ SEQUENCE 165 AA; 17720 MW; 3EB05150B80CDE95 CRC64;
MEQPLPTAAA EAAAAGGDGE AYRIRPLELA DISRGFLGLL NQLSPSPPLT EEAFRARFEE
LAALGADHLV LVAEDAATGR LAAAGAVLVE RKFIRRCGRV GHVEDVVVDA AARGRGLGER
VVRRLVEHAR GRGCYKVIIN CTPELTGFYA KCGFVEKNVQ MGLYF
