GNA1_YEAST
ID GNA1_YEAST Reviewed; 159 AA.
AC P43577; D6VTL3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase;
DE EC=2.3.1.4 {ECO:0000269|PubMed:9867860};
DE AltName: Full=Phosphoglucosamine acetylase;
DE AltName: Full=Phosphoglucosamine transacetylase;
GN Name=GNA1; Synonyms=PAT1; OrderedLocusNames=YFL017C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTAGENESIS, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9867860; DOI=10.1074/jbc.274.1.424;
RA Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.;
RT "Saccharomyces cerevisiae GNA1, an essential gene encoding a novel
RT acetyltransferase involved in UDP-N-acetylglucosamine synthesis.";
RL J. Biol. Chem. 274:424-429(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Barrell B.G., Churcher C., Rajandream M.A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH ACETYL-COENZYME A AND
RP THE SUBSTRATE GLUCOSAMINE-6-PHOSPHATE, AND SUBUNIT.
RX PubMed=11278591; DOI=10.1074/jbc.m009988200;
RA Peneff C., Mengin-Lecreulx D., Bourne Y.;
RT "The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1
RT shed light on the catalytic mechanism of an amino-sugar N-
RT acetyltransferase.";
RL J. Biol. Chem. 276:16328-16334(2001).
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:9867860};
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:0000269|PubMed:11278591}.
CC -!- MISCELLANEOUS: Present with 2550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB017626; BAA36495.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09221.1; -; Genomic_DNA.
DR EMBL; Z46255; CAA86352.1; -; Genomic_DNA.
DR EMBL; AY558564; AAS56890.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12423.1; -; Genomic_DNA.
DR PIR; S56237; S56237.
DR RefSeq; NP_116637.1; NM_001179949.1.
DR PDB; 1I12; X-ray; 1.30 A; A/B/C/D=1-159.
DR PDB; 1I1D; X-ray; 1.80 A; A/B/C/D=1-159.
DR PDB; 1I21; X-ray; 2.40 A; A/B/M/N/X/Y=1-159.
DR PDBsum; 1I12; -.
DR PDBsum; 1I1D; -.
DR PDBsum; 1I21; -.
DR AlphaFoldDB; P43577; -.
DR SMR; P43577; -.
DR BioGRID; 31130; 311.
DR DIP; DIP-1349N; -.
DR IntAct; P43577; 7.
DR MINT; P43577; -.
DR STRING; 4932.YFL017C; -.
DR iPTMnet; P43577; -.
DR MaxQB; P43577; -.
DR PaxDb; P43577; -.
DR PRIDE; P43577; -.
DR EnsemblFungi; YFL017C_mRNA; YFL017C; YFL017C.
DR GeneID; 850529; -.
DR KEGG; sce:YFL017C; -.
DR SGD; S000001877; GNA1.
DR VEuPathDB; FungiDB:YFL017C; -.
DR eggNOG; KOG3396; Eukaryota.
DR GeneTree; ENSGT00390000008666; -.
DR HOGENOM; CLU_072095_0_1_1; -.
DR InParanoid; P43577; -.
DR OMA; RGRGCYK; -.
DR BioCyc; MetaCyc:YFL017C-MON; -.
DR BioCyc; YEAST:YFL017C-MON; -.
DR Reactome; R-SCE-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; P43577; -.
DR UniPathway; UPA00113; UER00529.
DR EvolutionaryTrace; P43577; -.
DR PRO; PR:P43577; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43577; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IDA:SGD.
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; Acetylation; Acyltransferase; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..159
FT /note="Glucosamine 6-phosphate N-acetyltransferase"
FT /id="PRO_0000074552"
FT DOMAIN 28..159
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11278591"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11278591"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11278591"
FT BINDING 100..102
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:11278591,
FT ECO:0007744|PDB:1I12"
FT BINDING 108..113
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:11278591,
FT ECO:0007744|PDB:1I12"
FT BINDING 129..130
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11278591"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11278591"
FT BINDING 143..145
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:11278591,
FT ECO:0007744|PDB:1I12"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11278591"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 112..159
FT /note="GKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEMQIRK ->
FT ASS (in Ref. 4; CAA86352)"
FT /evidence="ECO:0000305"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:1I21"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1I12"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:1I12"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1I12"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1I12"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1I12"
FT STRAND 74..85
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1I12"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:1I12"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1I12"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:1I12"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:1I12"
SQ SEQUENCE 159 AA; 18135 MW; 2D2DD2D43A74C6F2 CRC64;
MSLPDGFYIR RMEEGDLEQV TETLKVLTTV GTITPESFSK LIKYWNEATV WNDNEDKKIM
QYNPMVIVDK RTETVAATGN IIIERKIIHE LGLCGHIEDI AVNSKYQGQG LGKLLIDQLV
TIGFDYGCYK IILDCDEKNV KFYEKCGFSN AGVEMQIRK
