GNA1_MIMIV
ID GNA1_MIMIV Reviewed; 148 AA.
AC Q5UPZ9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable glucosamine 6-phosphate N-acetyltransferase;
DE EC=2.3.1.4 {ECO:0000250|UniProtKB:Q96EK6};
DE AltName: Full=Phosphoglucosamine acetylase;
DE AltName: Full=Phosphoglucosamine transacetylase;
GN OrderedLocusNames=MIMI_L316;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
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:Q96EK6};
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}.
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DR EMBL; AY653733; AAV50586.1; -; Genomic_DNA.
DR RefSeq; YP_003986819.1; NC_014649.1.
DR SMR; Q5UPZ9; -.
DR GeneID; 9924933; -.
DR KEGG; vg:9924933; -.
DR UniPathway; UPA00113; UER00529.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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; Reference proteome; Transferase.
FT CHAIN 1..148
FT /note="Probable glucosamine 6-phosphate N-
FT acetyltransferase"
FT /id="PRO_0000074559"
FT DOMAIN 3..148
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 72..75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 86..88
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 94..99
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 129..131
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P43577"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
SQ SEQUENCE 148 AA; 17017 MW; 788C8C1D603F7BB7 CRC64;
MQISINELNF DDDSYQYMEL LKQLTYIDPS IITNEMFEKQ LSIIKNNPFH KIIVAKIDGK
IVGSTTVLIE PKFIHNLSSV GHIEDVVVDQ NYRLHGIGKL LIVKAIDICR QERCYKIILD
CSDKVCGFYC KLGFTPKEKQ MALYLNGK
