GNA1_CANAX
ID GNA1_CANAX Reviewed; 149 AA.
AC O93806;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase;
DE EC=2.3.1.4 {ECO:0000250|UniProtKB:P43577};
DE AltName: Full=Phosphoglucosamine acetylase;
DE AltName: Full=Phosphoglucosamine transacetylase;
GN Name=GNA1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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:0000250|UniProtKB:P43577};
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 -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017627; BAA36496.1; -; Genomic_DNA.
DR AlphaFoldDB; O93806; -.
DR SMR; O93806; -.
DR CGD; CAL0000198802; GNA1.
DR VEuPathDB; FungiDB:C2_03870W_A; -.
DR VEuPathDB; FungiDB:CAWG_04145; -.
DR UniPathway; UPA00113; UER00529.
DR PHI-base; PHI:174; -.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IMP:CGD.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:CGD.
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 3: Inferred from homology;
KW Acyltransferase; Transferase.
FT CHAIN 1..149
FT /note="Glucosamine 6-phosphate N-acetyltransferase"
FT /id="PRO_0000074551"
FT DOMAIN 7..149
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 76..79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 90..92
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 98..103
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 119..120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 133..135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
SQ SEQUENCE 149 AA; 16898 MW; 2C853F7D96F6C270 CRC64;
MMLPQGYTFR KLKLTDYDNQ YLETLKVLTT VGEISKEDFT ELYNHWSSLP SIYHPYVITN
ASGIVVATGM LFVEKKLIHE CGKVGHIEDI SVAKSEQGKK LGYYLVTSLT KVAQENDCYK
VILDCSPENV GFYEKCGYKD GGVEMVCRF
