GNA1_ARATH
ID GNA1_ARATH Reviewed; 149 AA.
AC Q9LFU9;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase;
DE EC=2.3.1.4 {ECO:0000269|PubMed:22329777};
DE AltName: Full=Glucose-6-phosphate acetyltransferase 1;
DE Short=AtGNA1;
DE AltName: Full=Phosphoglucosamine acetylase;
DE AltName: Full=Phosphoglucosamine transacetylase;
DE AltName: Full=Protein LIGNESCENS;
GN Name=GNA1; OrderedLocusNames=At5g15770; ORFNames=F14F8.150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-68.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22932674; DOI=10.1105/tpc.112.102806;
RA Nozaki M., Sugiyama M., Duan J., Uematsu H., Genda T., Sato Y.;
RT "A missense mutation in the glucosamine-6-phosphate N-acetyltransferase-
RT encoding gene causes temperature-dependent growth defects and ectopic
RT lignin deposition in Arabidopsis.";
RL Plant Cell 24:3366-3379(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22329777; DOI=10.1042/bj20112071;
RA Riegler H., Herter T., Grishkovskaya I., Lude A., Ryngajllo M.,
RA Bolger M.E., Essigmann B., Usadel B.;
RT "Crystal structure and functional characterization of a glucosamine-6-
RT phosphate N-acetyltransferase from Arabidopsis thaliana.";
RL Biochem. J. 443:427-437(2012).
CC -!- FUNCTION: Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-
CC GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves
CC as an initial sugar donor for N-glycan synthesis and thus plays an
CC important role in protein and lipid glycosylation.
CC {ECO:0000269|PubMed:22329777, ECO:0000269|PubMed:22932674}.
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:22329777};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for acetyl-coenzyme A {ECO:0000269|PubMed:22329777};
CC KM=231 uM for glucosamine-6-phosphate {ECO:0000269|PubMed:22329777};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:22329777};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:22329777};
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
CC {ECO:0000269|PubMed:22329777}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22329777}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, cauline leaves,
CC flowers and siliques. {ECO:0000269|PubMed:22329777}.
CC -!- DISRUPTION PHENOTYPE: Retarded vegetative growth, delayed flowering and
CC short and thick inflorescence stems and siliques.
CC {ECO:0000269|PubMed:22932674}.
CC -!- MISCELLANEOUS: The mutant lignescens (lig) was originally isolated as a
CC temperature-sensitive mutant that exhibits ectopic lignin deposition
CC and growth defects under high-temperature conditions.
CC {ECO:0000305|PubMed:22932674}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL391144; CAC01776.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92203.1; -; Genomic_DNA.
DR PIR; T51406; T51406.
DR RefSeq; NP_197081.1; NM_121582.2.
DR PDB; 3T90; X-ray; 1.50 A; A=1-149.
DR PDBsum; 3T90; -.
DR AlphaFoldDB; Q9LFU9; -.
DR SMR; Q9LFU9; -.
DR BioGRID; 16709; 3.
DR IntAct; Q9LFU9; 3.
DR STRING; 3702.AT5G15770.1; -.
DR PaxDb; Q9LFU9; -.
DR PRIDE; Q9LFU9; -.
DR ProteomicsDB; 247010; -.
DR DNASU; 831433; -.
DR EnsemblPlants; AT5G15770.1; AT5G15770.1; AT5G15770.
DR GeneID; 831433; -.
DR Gramene; AT5G15770.1; AT5G15770.1; AT5G15770.
DR KEGG; ath:AT5G15770; -.
DR Araport; AT5G15770; -.
DR TAIR; locus:2143226; AT5G15770.
DR eggNOG; KOG3396; Eukaryota.
DR HOGENOM; CLU_072095_3_0_1; -.
DR InParanoid; Q9LFU9; -.
DR OMA; NQRYDWI; -.
DR OrthoDB; 1479446at2759; -.
DR PhylomeDB; Q9LFU9; -.
DR BRENDA; 2.3.1.4; 399.
DR UniPathway; UPA00113; UER00529.
DR PRO; PR:Q9LFU9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFU9; differential.
DR Genevisible; Q9LFU9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:TAIR.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:TAIR.
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 3D-structure; Acyltransferase; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..149
FT /note="Glucosamine 6-phosphate N-acetyltransferase"
FT /id="PRO_0000421037"
FT DOMAIN 5..149
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 75..78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 97..102
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 132..134
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT MUTAGEN 68
FT /note="G->S: In lig; reduces activity 2-fold. Retarded
FT growth."
FT /evidence="ECO:0000269|PubMed:22932674"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:3T90"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3T90"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:3T90"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:3T90"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3T90"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:3T90"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3T90"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:3T90"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3T90"
SQ SEQUENCE 149 AA; 17028 MW; 209AF6CB83DCC857 CRC64;
MAETFKIRKL EISDKRKGFI ELLGQLTVTG SVTDEEFDRR FEEIRSYGDD HVICVIEEET
SGKIAATGSV MIEKKFLRNC GKAGHIEDVV VDSRFRGKQL GKKVVEFLMD HCKSMGCYKV
ILDCSVENKV FYEKCGMSNK SIQMSKYFD
