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Database: UniProt
Entry: J9VTF3_CRYNH
LinkDB: J9VTF3_CRYNH
Original site: J9VTF3_CRYNH 
ID   J9VTF3_CRYNH            Unreviewed;       761 AA.
AC   J9VTF3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   27-MAR-2024, entry version 47.
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=CNAG_01155 {ECO:0000313|EMBL:AFR94990.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94990.2, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR94990.2, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(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; CP003824; AFR94990.2; -; Genomic_DNA.
DR   RefSeq; XP_012049039.1; XM_012193649.1.
DR   AlphaFoldDB; J9VTF3; -.
DR   GeneID; 23884898; -.
DR   KEGG; cng:CNAG_01155; -.
DR   VEuPathDB; FungiDB:CNAG_01155; -.
DR   HOGENOM; CLU_009281_2_2_1; -.
DR   OrthoDB; 2734344at2759; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000010091; Chromosome 5.
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: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   PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 2.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 3.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:AFR94990.2};
KW   Transferase {ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          154..273
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          351..484
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          494..684
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  82378 MW;  16B58A836F9E27A4 CRC64;
     MSRPIDLSMS SVKNPSPLAA GGTGGFTPVF EASPANSPAG SRRPSISQPA ARRPSEVSVS
     RRPSVNQQYS SYMSQYPQQG VQSLSRRSSM ASGPRPIRRG EYSGPATPSV LSRAGSPTLP
     LGNEFTQAPR SYFEGASGYT PLGGTRELRN GQFIGSLDCG TTSTRFIIFD KRAKIIAEHQ
     TEFEQILPHA GWHEHDPEAL VEAMNECIIR AVEKLEWMGW SRNSIKGIGI TNQRETTVCW
     SRSTGKPLCN AIVWDDARTI NVVREMERKL DEEGLEIDDE EEDEINQKSE IVPDKVEMGT
     GTHEAAFGDK GDVVDGDTSM TGRIGKAMEG LGLAGRGKDG KAKKYRKGKE GLVDVTGIPL
     STYFSAIKLR WMLDHQKAVR VAHENDDLMF GTVDTWLVYN LTGAKNGGLH IIDVTNASRT
     LLVSLKTLRW HAPLLRFFGL RASILPKIVS SAEVYGNISD SLGLPLSGVP IAGIVGDQQA
     ALVGNKCLMK GQAKCTFGTG AFVLFNTGED IVRSNYGLIS TVAFQAGADS KPIYALEGSI
     AVAGSAIKWL RDQMTLIEES SEMDILAGSV SDTGGVYFVT AFSGLLAPYW DREAAGTIIG
     LTGYTTSAHI ARATLEAVCF QTRAVLDVIE KESGSRLDTL KVDGGVTNSD LAMQLQANIG
     GFNVARPSMR ESTALGSALL AAHALGLFGW DVTRPETLSE VNTAGVHTFE PELEEKARLK
     KIKGWNKAVD RAKKWHDIED EDEEEEEYEN EVGYARIAGS A
//
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