ID F9FMW8_FUSOF Unreviewed; 516 AA.
AC F9FMW8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=glycerol kinase {ECO:0000256|ARBA:ARBA00012099};
DE EC=2.7.1.30 {ECO:0000256|ARBA:ARBA00012099};
GN ORFNames=FOXB_07748 {ECO:0000313|EMBL:EGU81741.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU81741.1};
RN [1] {ECO:0000313|EMBL:EGU81741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU81741.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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}.
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:EGU81741.1}.
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DR EMBL; AFQF01002291; EGU81741.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FMW8; -.
DR STRING; 660025.F9FMW8; -.
DR UniPathway; UPA00618; UER00672.
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 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:SF75; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 13..267
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 277..466
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 516 AA; 56409 MW; B7299E8600938676 CRC64;
MPMLNGKPNP TFIGAIDQGT TSSRFLIFDT SGEVVATHQL EFKQYYPHPG WHEHDPEELI
SSVEQCIDGA VEAFEGQGHS REQIKAVGIT NQRETTVVWD KTTGNALHNA IVWTDTRSKD
LVRRLKRRLG ASELISRCGI PLSTYPSVSK LLWLLENIPE VKDAYERGVL AFGTVDTWLT
YKLNGATDRD VYVSDPSNAS RTMFMNLESL QYDEDILDWF RIDDKKITLP KIVRSSDSKA
YGTLAKTSLK GVKITGCLGD QSAALVGQKG FTPGLAKNTY GTGCFLLYNV GSKPVISTHG
LLTTVAFDFG EGNTMYALEG SIAVAGSSVK FLVDNFGFIE SSAKLSALAE TVEDNGGCTF
VTAFSGLFAP YWIDDARGTI FGITAYTQRG HVARATLEAT CFQTKAILDS MEKDSGHALT
ELAVDGGMCN SDLIMQTQSD LIGIPVNRPG MRETTALGAA IAAGFAVGIW KSFDELKEVN
TQGRTIFKPQ IAEEEATKRF SRWTKAVEMS KGWANE
//
