ID Q5KF71_CRYNJ Unreviewed; 1127 AA.
AC Q5KF71;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 2.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=glucosamine-phosphate N-acetyltransferase {ECO:0000256|ARBA:ARBA00012703};
DE EC=2.3.1.4 {ECO:0000256|ARBA:ARBA00012703};
GN OrderedLocusNames=CNF02770 {ECO:0000313|EMBL:AAW44278.2};
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:AAW44278.2, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW44278.2, 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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017346; AAW44278.2; -; Genomic_DNA.
DR RefSeq; XP_571585.1; XM_571585.1.
DR AlphaFoldDB; Q5KF71; -.
DR STRING; 214684.Q5KF71; -.
DR PaxDb; 214684-Q5KF71; -.
DR EnsemblFungi; AAW44278; AAW44278; CNF02770.
DR VEuPathDB; FungiDB:CNF02770; -.
DR eggNOG; KOG1449; Eukaryota.
DR eggNOG; KOG3396; Eukaryota.
DR HOGENOM; CLU_008682_1_1_1; -.
DR InParanoid; Q5KF71; -.
DR OrthoDB; 5482027at2759; -.
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:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039143; GNPNAT1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
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 Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 475..671
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 790..949
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 124564 MW; E8287A6531FC9DF6 CRC64;
MAYAYPSVDP LPEASSASLE IRPSKDPSRK NSDTLTDVFS EFKRKISEDE IYINFLQERV
RLENDYIEGL QRLYDRTVAI DSLHDEDPPP KRSEKPTSRK AWSEVRDYTL REIQAREAMK
GALEEDVIKE LTKLKDLQLK IRNYLKQNIK LAEHMYEDHA KHQLPKLKKA YFQKSQVLED
HRRQENAIAT QARLLSSAPP PSPTSTPLQE HPFSVGTGAS YALPSTIISP LPPVNNPAAS
SVSKVSSQET TSGMFVPSPN KDREKEMKFG NRLRAESGSG LENKSRDVLN DIATHGKKGF
SAFMQRLGGD KDREREKDDV QITSHGVEGE GLQRRGTTGS ANIKAQMAVR GAKAKREADE
ADRAYRMGIF HLESLRLRTE KLHSSAITHL EEFNDELSNK LRRAMVAYVD IMHSTAMTSA
QATEVARIAI DTIDADHDMM LFRKRLLVAT SNTTKAPVPY ENFYVGPCRS LIFGVSLTDY
DFARGDGNDH GSPPMIVEKC IAAIDARGLE AEGIYRVNGR HTGVQKMVQD IEKDETQFEF
GEKDDVFSIA SVLKQYLREL PEPVFNLPHA ERVKYSKHRE LHISNNFSAI RGRLRRLPPI
HQTTFQSIIE HLGRVHEKRG MNKMGAKNLA VLFSSVLFGQ EQAPSDGNVL MMNQEADTVL
EDLITFSNLL FGGIGSPKTS HILPSSLAFS SGVNAEVSVI DDPQPGSSHT KIKILQQETT
PQRLVDHSAQ ISDKDQRATD ETDDYRPNTL QDTETVQTLL EDFPSNKDLD LLFDAKLLPS
SMRENLPKDI EVRPLASTDL LRQHFELLSN LRPSPALAPS LYQAIFTHFK SCPLTYYTVV
MVDTKIDRLV ASGTLLVERK HINGGSAAGH LEDIVVAEEM RGKKLGVKLV TGLRDLAVSL
GCYKVVLDCK EAKIPFYENC GFHKRSAGMA YYTPSDQGTA HVSFSTQSNQ QSLLPYAPND
SLAPPVSTMG TLTPGTELNI TPQMNQSLHD PLSQSDVTSD DQKGILLTIP DGTAASDGES
PGSPRTFTSA SSEAGMGVTY DFPTAVDESV LPAWAAEGLG GNTSHVSDRR ASDKTESTLP
AFSILEGVGV AKSKDSEAAD DSKEGRSRTP FPSRVASSDS TTETSSK
//
