ID A0A3F3PVQ8_9EURO Unreviewed; 693 AA.
AC A0A3F3PVQ8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BDQ94DRAFT_180946 {ECO:0000313|EMBL:RDH30928.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH30928.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH30928.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH30928.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC family. {ECO:0000256|ARBA:ARBA00006198}.
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; KZ852058; RDH30928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PVQ8; -.
DR STRING; 1341132.A0A3F3PVQ8; -.
DR OrthoDB; 7403at2759; -.
DR Proteomes; UP000253729; 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; -; 2.
DR HAMAP; MF_00068; MurQ; 1.
DR InterPro; IPR002731; ATPase_BadF.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR005488; Etherase_MurQ.
DR InterPro; IPR005486; Glucokinase_regulatory_CS.
DR InterPro; IPR040190; MURQ/GCKR.
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; 2.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 60..226
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 693 AA; 73330 MW; E3C8420024ABC635 CRC64;
MAQDVLDLSG LQTEAINEHT SNIDRVSTLQ MCTMINDEDK TVAESVTACL EDIALAIDLL
VPRVRVGGRV IYVGAGTSGR LGILDSSEIL PTFAAPPTQF VGLIAGGDAA IREAQEGAED
SITAGKDDLA AMNLNGEQDS IIGIAASGRT PYVLGALEYA KSLGCLTLGV ACVSPSEMGQ
SGNLDIMIAP LPGAEVVTGS TRLKAGTATK LVLNMLSTGT MIKAGKTYGN MMIDLIASNQ
KLKQRSRNIL RRVSRRCSTM TDEDLDDLLA RCGGRVKVAL LVADKGVSVE ESREQLEMAQ
GVLAKVIATE DKAPVKTPLI NGFKHHRSAL CIDGGGSKCA AVVGDTSGNI GKGVAGPCNL
RTDGEFEASV DAIVTAAREA FGNIPNSTNH INGINDSTDP HLSFITNHGK SFDSIWIASA
GMDRPGMRER VQAAVAQRLN LNKSIQMRVT NDVDLLAAAM TRHPEISSSL VVIAGTGSIA
IRYAYNNDDI VPRRVARTGG WGHLLGDEGA GYAIGRQAIR KTLFSLDNIK LARQKSGLST
LGLKIVNIFS NYSSKENDDA LDIDLLSNVL MASEDKSAKS RIAGIAQTIL DLAGSGDAEA
VGIIAQQVTR FVDNTLTRLL DPQSHGYVDP SKCGLILSGG VMLHTVYQTI FQLALAKRNI
RFSYTEAVPN AAMVGVEYLL ASHTLRPLQN GVS
//
