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Database: UniProt
Entry: A0A1V6QEY4_9EURO
LinkDB: A0A1V6QEY4_9EURO
Original site: A0A1V6QEY4_9EURO 
ID   A0A1V6QEY4_9EURO        Unreviewed;       586 AA.
AC   A0A1V6QEY4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=glycerol kinase {ECO:0000256|ARBA:ARBA00012099};
DE            EC=2.7.1.30 {ECO:0000256|ARBA:ARBA00012099};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|ARBA:ARBA00043149};
GN   ORFNames=PENANT_c005G02531 {ECO:0000313|EMBL:OQD87780.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD87780.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005190}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU003733}.
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:OQD87780.1}.
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DR   EMBL; MDYN01000005; OQD87780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QEY4; -.
DR   STRING; 416450.A0A1V6QEY4; -.
DR   OrthoDB; 2734344at2759; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07795; FGGY_ScGut1p_like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   NCBIfam; TIGR01311; glycerol_kin; 1.
DR   PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Kinase {ECO:0000256|RuleBase:RU003733};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Transferase {ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          70..324
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          334..524
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  64787 MW;  C24F2DBAB0AF0740 CRC64;
     MRNPFELDYD SVDGDSEPAG DFELSEAQLP QEGHHRRSSL DYRPKQQDDG DRSLLQNEDK
     IPGDLKNRFI GTIDQGTTST RFIIFDCTGV PVAKYQTEFR QIHEHPGWHE QDPYELVESV
     YICMEEAMKS FLAAGHDASD IEAVGITSQR ETALVWDWET GEPLHNAITW TDTRTVNLVR
     ELKAKPGADE LANICGLPLS TYPSSVTLRW MLDHLPDVKS AYDDGRAAFG TVDSWLIYNL
     NGGPQNKRLV TDVTNASRTM FMNLETLKYD DRLLKFFDID KTKIRLPEIL PSADPEGFGR
     IVEGPLDGVR ITSCLGDQAS ALVGHCAFTP GMAKNTYGTG CFLLYNVGDK PVISKHGLLG
     TVGFQLGRDR KPVYALEGSV AVAGSGVSFL MNNLGFFRDS RKVSDLAASV PDNGGCIFVT
     AFSGLFAPYW IDDAQGTIWG ITAHTQKGHI ARATMEAACF QTKAILDAMA MDSGKSLTEL
     AVDGGMSNSD VCMQTQADII QIPVERPSMH ETTALGAAIA AGFAVDIWKD FSELKHMNRA
     NRASFTPQMT PKASGRMYKK WSKAVEMSRG WMNDEDRMEH DEDDDE
//
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