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Database: UniProt
Entry: C5NZL9_COCP7
LinkDB: C5NZL9_COCP7
Original site: C5NZL9_COCP7 
ID   C5NZL9_COCP7            Unreviewed;       510 AA.
AC   C5NZL9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=glycerol kinase {ECO:0000256|ARBA:ARBA00012099};
DE            EC=2.7.1.30 {ECO:0000256|ARBA:ARBA00012099};
GN   ORFNames=CPC735_012300 {ECO:0000313|EMBL:EER29912.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29912.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER29912.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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   -!- 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:EER29912.1}.
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DR   EMBL; ACFW01000001; EER29912.1; -; Genomic_DNA.
DR   RefSeq; XP_003072057.1; XM_003072011.1.
DR   AlphaFoldDB; C5NZL9; -.
DR   GeneID; 9697552; -.
DR   KEGG; cpw:CPC735_012300; -.
DR   VEuPathDB; FungiDB:CPC735_012300; -.
DR   HOGENOM; CLU_009281_2_3_1; -.
DR   OrthoDB; 2734344at2759; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000009084; 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: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, ECO:0000313|EMBL:EER29912.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:EER29912.1}.
FT   DOMAIN          9..263
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          273..461
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   510 AA;  55965 MW;  130B2652F46D26A3 CRC64;
     MAKDIESFIG SIDQGTTSSR FLIFNKNGEV VASHQLEFTQ IYPQPGWHEH DPKEIVTSVE
     RCIDGAVSSF EHQGYNVESI KAVGITNQRE TTVVWDKETG EPLYNAIVWT DTRTQSLIRR
     LKRRLGHGEV HEHCGLPLST YPSVGKLLWL LENVPKVKDA YEKGVLAFGT IDTWLVYMLN
     GGPKKNVFVT DPSNASRTMF MNIRTRQYDE TLIDFFRLDE GKLHLPKIIS SSDPTGYGSL
     ASTVLKGVPI TGCLGDQSAA LVGQKGFTPG KAKNTYGTGC FLLYNVGEKP VISRHGLLTT
     VAFDFGGQAM YALEGSIAVA GSSVKFLKDN FEFISSSDEV NKLAETVEDN GGCVFVTAFS
     GLFAPYWMDD ARGTIFGITT YTKRGHIARA TLEATCFQTK AILDAMSKDS GHALTELAVD
     GGMCNSDLTM QTQADLISIP VIRPAMRETT AFGAAIAAGL AVGLWEGIEE LQNVNTDGQT
     VFRPSIQKEE AEERFLRWEK AVRMCQGWSG
//
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