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Database: UniProt
Entry: V4B605_LOTGI
LinkDB: V4B605_LOTGI
Original site: V4B605_LOTGI 
ID   V4B605_LOTGI            Unreviewed;       193 AA.
AC   V4B605;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Glucosamine 6-phosphate N-acetyltransferase {ECO:0000256|RuleBase:RU365086};
DE            EC=2.3.1.4 {ECO:0000256|RuleBase:RU365086};
GN   ORFNames=LOTGIDRAFT_212480 {ECO:0000313|EMBL:ESP02946.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP02946.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESP02946.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
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; KB200129; ESP02946.1; -; Genomic_DNA.
DR   RefSeq; XP_009046416.1; XM_009048168.1.
DR   AlphaFoldDB; V4B605; -.
DR   STRING; 225164.V4B605; -.
DR   EnsemblMetazoa; LotgiT212480; LotgiP212480; LotgiG212480.
DR   GeneID; 20246366; -.
DR   KEGG; lgi:LOTGIDRAFT_212480; -.
DR   CTD; 20246366; -.
DR   HOGENOM; CLU_072095_1_0_1; -.
DR   OMA; SGNIMNQ; -.
DR   OrthoDB; 1341425at2759; -.
DR   UniPathway; UPA00113; UER00529.
DR   Proteomes; UP000030746; 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:UP000030746};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365086}.
FT   DOMAIN          47..193
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   193 AA;  22198 MW;  9F486072D1454589 CRC64;
     MSVSHGIVEK RGDTPIYNST ILDSVDFNRH RASFNPPITP DNLGEEFVMR PLCLEDFERG
     YMELLDEHVP NGLINKEEFT ERFNKMKKAG DIHLITVIED VTTNKTIASA TLVNELKFLM
     KATSRGRIED VVVSKPYRGK QFGKILLETL TLLAEKLGCY ESSLECEQKN ITYYSKFGYQ
     VEPNDQYMTL RFK
//
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