ID J4G6F2_9APHY Unreviewed; 164 AA.
AC J4G6F2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, 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=FIBRA_03845 {ECO:0000313|EMBL:CCM01778.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM01778.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM01778.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM01778.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797049; CCM01778.1; -; Genomic_DNA.
DR RefSeq; XP_012181061.1; XM_012325671.1.
DR AlphaFoldDB; J4G6F2; -.
DR STRING; 599839.J4G6F2; -.
DR GeneID; 24096689; -.
DR HOGENOM; CLU_072095_0_1_1; -.
DR InParanoid; J4G6F2; -.
DR OrthoDB; 1341425at2759; -.
DR UniPathway; UPA00113; UER00529.
DR Proteomes; UP000006352; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU365086};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365086}.
FT DOMAIN 75..135
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00583"
SQ SEQUENCE 164 AA; 18413 MW; 77AFFF2A105EA934 CRC64;
MPFTPDSELD LLFPAEHIPD ETKKQLPSDL HLRPLASTDY KRGHLSVLSV LTVVTDPGEG
AWVTQFNAIR AASRTYYSIV IVDKPSDRIV AVGTVFIERK FLRGLGSVGH IEDIAVDKSQ
QGKKLGLRII QALTGITFYQ KCGFERKENE MTRYAPDRSR SPRL
//
