GNA1_DICDI
ID GNA1_DICDI Reviewed; 157 AA.
AC Q54WR8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase 1;
DE Short=GNPNAT1;
DE EC=2.3.1.4 {ECO:0000250|UniProtKB:Q96EK6};
GN Name=gna1; ORFNames=DDB_G0279475;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000031; EAL67676.1; -; Genomic_DNA.
DR RefSeq; XP_641649.1; XM_636557.1.
DR AlphaFoldDB; Q54WR8; -.
DR SMR; Q54WR8; -.
DR STRING; 44689.DDB0304953; -.
DR PaxDb; Q54WR8; -.
DR EnsemblProtists; EAL67676; EAL67676; DDB_G0279475.
DR GeneID; 8622056; -.
DR KEGG; ddi:DDB_G0279475; -.
DR dictyBase; DDB_G0279475; gna1.
DR eggNOG; KOG3396; Eukaryota.
DR HOGENOM; CLU_072095_0_1_1; -.
DR InParanoid; Q54WR8; -.
DR OMA; NQRYDWI; -.
DR PhylomeDB; Q54WR8; -.
DR Reactome; R-DDI-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00529.
DR PRO; PR:Q54WR8; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; ISS:dictyBase.
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; ISS:dictyBase.
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..157
FT /note="Glucosamine 6-phosphate N-acetyltransferase 1"
FT /id="PRO_0000393569"
FT DOMAIN 9..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 78..81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 90..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 100..105
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 121..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 135..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
SQ SEQUENCE 157 AA; 17994 MW; E126FB6E29CDC817 CRC64;
MSSIVDDGIS FRPLDIDDFD KGYSECLQQL TEAKFTKEQF IERFNQIKKQ SDTYFLIVAV
DVKLNKIIAC GSLFVEKKFI RNCGKCGHIE DIVVNNNYRG KNLGLRIIEQ LKCIGSQAGC
YKIILDCSEA NVKFYEKCKF ERKGVQMSIY LPTPPKL
