ID A0A015J5M7_RHIIW Unreviewed; 170 AA.
AC A0A015J5M7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase {ECO:0000256|RuleBase:RU365086};
DE EC=2.3.1.4 {ECO:0000256|RuleBase:RU365086};
GN ORFNames=RirG_273110 {ECO:0000313|EMBL:EXX50204.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX50204.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX50204.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) 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:0000256|ARBA:ARBA00000866,
CC ECO:0000256|RuleBase:RU365086};
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 {ECO:0000256|ARBA:ARBA00004832, ECO:0000256|RuleBase:RU365086}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000256|ARBA:ARBA00006048, ECO:0000256|RuleBase:RU365086}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXX50204.1}.
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DR EMBL; JEMT01030157; EXX50204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015J5M7; -.
DR STRING; 1432141.A0A015J5M7; -.
DR HOGENOM; CLU_072095_0_1_1; -.
DR OMA; EHEMARY; -.
DR UniPathway; UPA00113; UER00529.
DR Proteomes; UP000022910; Unassembled WGS sequence.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039143; GNPNAT1-like.
DR PANTHER; PTHR13355; GLUCOSAMINE 6-PHOSPHATE N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR13355:SF11; GLUCOSAMINE 6-PHOSPHATE N-ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU365086};
KW Reference proteome {ECO:0000313|Proteomes:UP000022910};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365086}.
FT DOMAIN 25..170
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 170 AA; 19279 MW; BC9EABD1606FD46D CRC64;
MSTQKNLFST DLISPEVQAS LPKGYTLRPL SIDDYELGFF EVLSVFEDIG NLSKDQFLER
FNYMRARNDE YFIIVIISPE NRIVGTGTIF VERKFIFNAG LVGHIEDVAI DKNHQGKHFG
SSIVQALKYI GIKTGCIKAI LDCSVENISF YEKCGLQNRG IEMSCDFDTR
//
