ID C4Y113_CLAL4 Unreviewed; 628 AA.
AC C4Y113;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=CLUG_01895 {ECO:0000313|EMBL:EEQ37772.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ37772.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ37772.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ37772.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408077; EEQ37772.1; -; Genomic_DNA.
DR RefSeq; XP_002618436.1; XM_002618390.1.
DR AlphaFoldDB; C4Y113; -.
DR STRING; 306902.C4Y113; -.
DR GeneID; 8498952; -.
DR KEGG; clu:CLUG_01895; -.
DR VEuPathDB; FungiDB:CLUG_01895; -.
DR HOGENOM; CLU_009281_2_2_1; -.
DR InParanoid; C4Y113; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 2734344at2759; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000007703; 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 Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 94..347
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 356..569
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 68971 MW; CD0F1E9978DBA34E CRC64;
MPRRSSTAPS APVVATIDIG TTSARCILFS KDGTEVAKHQ IEYSTSASEA PAESSNTDQF
RRRSSLARHN EPIFTAEGVA ISISDHVEIE NNAASVGPTL RFPQPGWVEC MPVHILANAV
QCLVACLITL RKINQNPDLK IKYKVKCIGI ANMRETTIVW DRKTGKPLSN GITWTDTRTA
EIVHHLENMT DDETKARMKE KTGLPLSTYF SAAKLRWLLD NDDTIRELYE KGDNLMFGTV
DTWLIYHLTK ERTFVTDVTN ASRTSFMNLE TRDYDDELLD FWGIDPSKIS MPKIVSSSEF
YGSFVAPNLS SLGFHNRITQ EAYDMLKTIY NVPICGCLGD QSASLVGQLA VKAGSAKCTY
GTGCFLLYNT GVRRLTSNNG ALTTLGFWFP TLGGEDGQPH YALEGSVAVA GSIIQWLRDN
LKLIESAKDI GPLASQASNS GGVVFIPAFS GLYAPYWDGG ARGTIFGMTQ YTSSAHIARA
ALEGVCFQVR GILRAMSEDA GGSKDFLEEA LHSQHEDKPL STLAVDGGMS KAGEVLQIQA
DILGPCVTVK RAAISECTAL GAAIAAGVSF KDENERVWRD FEDVIQSVTG EDDEANVFKA
KLPDVDRRKN WRRWERAVER AKGWLDEE
//