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Database: UniProt
Entry: A0A0M3JZX2_ANISI
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Original site: A0A0M3JZX2_ANISI 
ID   A0A0M3JZX2_ANISI        Unreviewed;       242 AA.
AC   A0A0M3JZX2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glucosamine 6-phosphate N-acetyltransferase {ECO:0000256|RuleBase:RU365086};
DE            EC=2.3.1.4 {ECO:0000256|RuleBase:RU365086};
GN   ORFNames=ASIM_LOCUS13514 {ECO:0000313|EMBL:VDK49906.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001408601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001408601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK49906.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYRR01031415; VDK49906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M3JZX2; -.
DR   WBParaSite; ASIM_0001408601-mRNA-1; ASIM_0001408601-mRNA-1; ASIM_0001408601.
DR   UniPathway; UPA00113; UER00529.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; 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   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:UP000267096};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365086}.
FT   DOMAIN          95..242
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   242 AA;  27472 MW;  FF419C594B833DA3 CRC64;
     MEGVGMDACA RKLREETDCL DCAEDKPSSR LNNNNNNNNN CLTDIDYSLC SELVALSRIL
     TPVVDYISDD VDMFPLEVLS SLHLPLSAPK LPADLIVRPL RSTDYNHGYL QLLSQLTSVG
     DVSEEQFHKR FLSMQKTNPK SYYVVVLEEI SSGMLVGSAT LVIEWKFIHE AGCRGRTEDV
     VVDRRMRGKQ LGKLLNFYLV ELARLIGVYK MSLECKDSLI PFYEQFGFKL DQGNNFLVQR
     FD
//
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