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Database: UniProt
Entry: A0A074WQU5_9PEZI
LinkDB: A0A074WQU5_9PEZI
Original site: A0A074WQU5_9PEZI 
ID   A0A074WQU5_9PEZI        Unreviewed;       574 AA.
AC   A0A074WQU5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=M437DRAFT_64425 {ECO:0000313|EMBL:KEQ64801.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ64801.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ64801.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ64801.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU003733}.
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DR   EMBL; KL584828; KEQ64801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074WQU5; -.
DR   STRING; 1043003.A0A074WQU5; -.
DR   HOGENOM; CLU_009281_2_3_1; -.
DR   OrthoDB; 2734344at2759; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000030672; Unassembled WGS sequence.
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; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:KEQ64801.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW   Transferase {ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          64..318
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          328..518
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  63006 MW;  F76540A816D749E5 CRC64;
     MGSLSGNPNV DQISEQPADP TLKKASAATD AKPKVRTESK SGAQRPPLNR FTTSHENVLH
     EHFIGAIDQG TTSSRFIIFD GVGEPVAMHQ IEFEQKYPES GWHEHDPWEL VASVETCIEE
     ATKKFLEKGH KVSDIKAIGL TNQRETTLVW DAETGQPLHN AIAWPDTRTK GLVREFKERK
     GDQNLSEICG IPLSTYPSCL KLVWMLRHVP EVQQAYDEGR LCFGTVDTWL IYNLNGGKEK
     NIFVTDSTNA SRTMFMNLHT CQYDDNLLSF FDLDRNKLRL PKIVPSSCAD AYGSLAKGIL
     KGMKIAGCLG DQSSALVGQQ GFTPGSAKNT YGTGCFLLYN VGEKPTISTH GLLATVAYDF
     GRNRKPVYAL EGSVAVAGSG VKFLMNNMGF IAHAEKVSEL ASTVDDNGGL VFVTAFSGLF
     APYWIDDAKG TIFGITQHTQ RGHIARATLE ATCFQTKAIL DAMEKDSGHA LSDLAVDGGM
     SNSNICMQTQ ANIIGIPVNR PAMRETTALG AAIAAGFAVD IWKEFSELKA INQKNRMVFE
     PEVTPEESEK MFKKWDRAVS MCRGWLDVDE VTET
//
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