ID A0A0T5ZDG8_9ARCH Unreviewed; 145 AA.
AC A0A0T5ZDG8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=glucosamine-phosphate N-acetyltransferase {ECO:0000256|ARBA:ARBA00012703};
DE EC=2.3.1.4 {ECO:0000256|ARBA:ARBA00012703};
GN ORFNames=XU09_C0008G0336 {ECO:0000313|EMBL:KRT60866.1};
OS Thaumarchaeota archaeon CSP1-1.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT60866.1, ECO:0000313|Proteomes:UP000051388};
RN [1] {ECO:0000313|EMBL:KRT60866.1, ECO:0000313|Proteomes:UP000051388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT60866.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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 -!- 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:KRT60866.1}.
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DR EMBL; LDXL01000008; KRT60866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZDG8; -.
DR STRING; 1640512.XU09_C0008G0336; -.
DR Proteomes; UP000051388; 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:KRT60866.1}.
FT DOMAIN 4..145
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 145 AA; 16497 MW; 12914FEED3991882 CRC64;
MVDITIRELE EKDLFNGFLQ SMDSLKPASN IDKEKAIEIY NKIKSNPNHL VYVAILGERV
VGSTTMLIEP KFIHDGGNVS HIEDVVVSKE YQGKGIGEML VQSLLDLAKD NNCYKTILDC
SDEVKPFYEK IGFIRHSNGM RYDHF
//
