ID A0A150J4B0_9EURY Unreviewed; 150 AA.
AC A0A150J4B0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=glucosamine-phosphate N-acetyltransferase {ECO:0000256|ARBA:ARBA00012703};
DE EC=2.3.1.4 {ECO:0000256|ARBA:ARBA00012703};
GN ORFNames=AMQ22_01002 {ECO:0000313|EMBL:KYC52059.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC52059.1, ECO:0000313|Proteomes:UP000075398};
RN [1] {ECO:0000313|EMBL:KYC52059.1, ECO:0000313|Proteomes:UP000075398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U1lsi0528_Bin055 {ECO:0000313|EMBL:KYC52059.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000256|ARBA:ARBA00006048}.
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:KYC52059.1}.
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DR EMBL; LNGC01000035; KYC52059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150J4B0; -.
DR STRING; 1705564.APG08_00913; -.
DR Proteomes; UP000075398; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KYC52059.1}.
FT DOMAIN 2..150
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 150 AA; 17298 MW; A2C14B83971278C0 CRC64;
MLRVREASFR DRYNIYDLID SLHNVPLKSP DEIANFNKIL TEYIKNPNIK IFVAEENLLD
SVEICGFLSL FVKPILFYSY NVCHIEDIVI KDEYKGKGVG AELLEAAINY GKRVKCKYIT
VSIEGGDPMT KKFYKACGFA ENSLEMKYYL
//
