ID Q5KF35_CRYNJ Unreviewed; 186 AA.
AC Q5KF35; Q55R34;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase {ECO:0000256|RuleBase:RU365086};
DE EC=2.3.1.4 {ECO:0000256|RuleBase:RU365086};
GN OrderedLocusNames=CNF03220 {ECO:0000313|EMBL:AAW44088.2};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW44088.2, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW44088.2, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017346; AAW44088.2; -; Genomic_DNA.
DR RefSeq; XP_571395.1; XM_571395.1.
DR AlphaFoldDB; Q5KF35; -.
DR STRING; 214684.Q5KF35; -.
DR PaxDb; 214684-Q5KF35; -.
DR EnsemblFungi; AAW44088; AAW44088; CNF03220.
DR VEuPathDB; FungiDB:CNF03220; -.
DR eggNOG; KOG3396; Eukaryota.
DR HOGENOM; CLU_072095_0_1_1; -.
DR InParanoid; Q5KF35; -.
DR OrthoDB; 1341425at2759; -.
DR UniPathway; UPA00113; UER00529.
DR Proteomes; UP000002149; Chromosome 6.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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 ECO:0000256|RuleBase:RU365086};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365086}.
FT DOMAIN 28..183
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 186 AA; 20533 MW; D5E4CA7069E2D21A CRC64;
MTPDSSLDLL FDPSILPASA QDELGPDLYL RPLSSTDVLR GHIELLSVLT SAPPQSVSTY
ETIFQEMKAS AGIYFTVVVV HRLSNQVVAC GSVIIERKFV RNAGLVGHIE DIAVSQSMQG
RKLGMKIINT LVDIGLARGC YKIILDCSEK NIPFYEKCGF KQKEFQMVRY LLDPSDVVKV
PTPSKL
//
