ID J5J586_BEAB2 Unreviewed; 645 AA.
AC J5J586;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000256|ARBA:ARBA00014974};
DE EC=2.7.1.59 {ECO:0000256|ARBA:ARBA00012122};
DE AltName: Full=GlcNAc kinase {ECO:0000256|ARBA:ARBA00031123};
GN ORFNames=BBA_09315 {ECO:0000313|EMBL:EJP61753.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP61753.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP61753.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP61753.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC family. {ECO:0000256|ARBA:ARBA00006198}.
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DR EMBL; JH725199; EJP61753.1; -; Genomic_DNA.
DR RefSeq; XP_008602634.1; XM_008604412.1.
DR AlphaFoldDB; J5J586; -.
DR STRING; 655819.J5J586; -.
DR GeneID; 19892327; -.
DR HOGENOM; CLU_022562_0_0_1; -.
DR InParanoid; J5J586; -.
DR OrthoDB; 7403at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:InterPro.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046348; P:amino sugar catabolic process; IEA:InterPro.
DR CDD; cd05007; SIS_Etherase; 1.
DR Gene3D; 1.10.8.1080; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR HAMAP; MF_00068; MurQ; 1.
DR InterPro; IPR002731; ATPase_BadF.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR005488; Etherase_MurQ.
DR InterPro; IPR040190; MURQ/GCKR.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1.
DR PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1.
DR Pfam; PF01869; BcrAD_BadFG; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS50012; RCC1_3; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000313|EMBL:EJP61753.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transferase {ECO:0000313|EMBL:EJP61753.1}.
FT DOMAIN 60..226
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REPEAT 68..116
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
SQ SEQUENCE 645 AA; 67962 MW; 47BEE2E668006B64 CRC64;
MPPSGVDLGG LQTENSNPRT ATIDKVSTEE LCRILHEEDC RVPAAVTPCL PEIAATIDAL
TERVRKGGRV FYIGAGTSGR LGVLDASEIP PTYSSPPNQF IALIAGGDYA LRNAKEGAED
DRSAAKTDLD AFNIAPNLDS LIGIASSGRT PYVLGGLEYA RSIGCTTVGV VCVQPSAMAI
EGNTDYLISA VTGSESVTGS TRMKAGTATK LVLNMISTGI MIKLGKTYGN LASLRMVDLK
ATNIKLRQRA RNILRVIGGQ RCHHSDQELD AILATARGST RLAAVMMVLD VPLVEAELRL
DRNNGVLDRV FTEAETQSRG TSCKATILSK DGAVGAGFGG PCNVIAGAIQ QATDSCPTTK
GRVFSSIKFA AARIGLAGYD RPAVQSSVND GLSKLLNLKI GAGLEVTTDI DLLPVASASE
ETVECAVVLV AGTGSIAMSF RKENGAFVRS GRAGGWGHLL GDDGSGYSIG REALRMALRE
SDVCSMRKQA SAPAQPTSQL AKAVFGHFKE KFPEAKPEDL LSTVMMPNSA PQQPRDAVMD
RTSRIAGVAK TVLAMVKTNE DADRIVAAGA EKLAELAALL VLNQGIKPSK ASLVLAGGLM
QDEGYRRRIV GSVERAGYKF QHVEVVDQPA MNGARFLLRS AQTLQ
//
