GNA1_PONAB
ID GNA1_PONAB Reviewed; 184 AA.
AC Q5RAL9; Q5NVB8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=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 Name=GNPNAT1; Synonyms=GNA1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96EK6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC protein. Endosome membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RAL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RAL9-2; Sequence=VSP_016537;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91191.1; Type=Miscellaneous discrepancy; Note=Erroneous pre-mRNA splicing.; Evidence={ECO:0000305};
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DR EMBL; CR858996; CAH91191.1; ALT_SEQ; mRNA.
DR EMBL; CR926120; CAI29745.1; -; mRNA.
DR RefSeq; NP_001125698.1; NM_001132226.1.
DR AlphaFoldDB; Q5RAL9; -.
DR SMR; Q5RAL9; -.
DR STRING; 9601.ENSPPYP00000006615; -.
DR Ensembl; ENSPPYT00000006878; ENSPPYP00000006615; ENSPPYG00000005822. [Q5RAL9-1]
DR GeneID; 100172622; -.
DR KEGG; pon:100172622; -.
DR CTD; 64841; -.
DR eggNOG; KOG3396; Eukaryota.
DR GeneTree; ENSGT00390000008666; -.
DR HOGENOM; CLU_072095_1_0_1; -.
DR InParanoid; Q5RAL9; -.
DR OMA; NQRYDWI; -.
DR OrthoDB; 1479446at2759; -.
DR TreeFam; TF313790; -.
DR UniPathway; UPA00113; UER00529.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Endosome; Golgi apparatus; Membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..184
FT /note="Glucosamine 6-phosphate N-acetyltransferase"
FT /id="PRO_0000074555"
FT DOMAIN 39..184
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 108..111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 130..135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 165..167
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016537"
FT CONFLICT 88
FT /note="V -> I (in Ref. 1; CAI29745)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="C -> S (in Ref. 1; CAH91191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 20749 MW; E9F31803CF633BBF CRC64;
MKPDETPMFD PSLLKEVDWS QNTATFSPAI SPTHPGEGLV LRPLCTADLN RGFFKVLGQL
TETGVVSPEQ FMKSFEHMKK SGDYYVTVVE DVTLGQIVAT ATLIIEHKFI HSCAKRGRVE
DVVVSDECRG KQLGKLLLST LTLLSKKLNC YKITLECLPQ NVGFYKKFGY TVSEENYMCR
RFLK
