ID J3KJI0_COCIM Unreviewed; 642 AA.
AC J3KJI0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 40.
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=CIMG_01582 {ECO:0000313|EMBL:EAS36228.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS36228.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
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).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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}.
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DR EMBL; GG704911; EAS36228.3; -; Genomic_DNA.
DR RefSeq; XP_001247811.2; XM_001247810.2.
DR AlphaFoldDB; J3KJI0; -.
DR STRING; 246410.J3KJI0; -.
DR GeneID; 4567321; -.
DR KEGG; cim:CIMG_01582; -.
DR VEuPathDB; FungiDB:CIMG_01582; -.
DR InParanoid; J3KJI0; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 2734344at2759; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001261; 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 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, ECO:0000313|EMBL:EAS36228.3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 133..386
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 396..586
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 642 AA; 70335 MW; 50D39C4667DC8894 CRC64;
MYNSLVSLPA EKGMLPITAF QSLCQYNPFL SSIQSVPLKF YNLPQIYCLE NRFLCRIPQF
VLPKFALAER SRIITSRINL SKVIGDLGMA GATVMPIRSQ LGRDIDSSQV SQATPARGPF
IADHSKPQRR FVGAIDQGTT STRFIIFDDQ GNLVASYQTE LSRLHKYPGW HEQDPKEIIS
SVESCIAQAT KTFVNLGHSI SDIQALGITN QRETTVVWDW ETGEPLHSAI AWPDTRTASL
VRELKSKEGA DQLQEKCGLP LSTYPSSVKL TWLLRNCKEV KEAYEAGRLA FGTVDTWLLY
NLNGGRKRGV FVTDVTNASR TMFTNLHTLQ YDDSLLKFFD IDRSKLKLPK ILASSDESAF
GCMADGLLAG IRITSCLGDQ SASLVGHGAL TPGTAKNTYG TGCFLLYNVG ETPVISKHGL
LATVAFQLGS KQKPIYALEG SIAVAGSGVS FLMNNLGFFR DSRKVDEEAA TVPDNGGCIF
VTAFSGLFAP YWVDDAKGTI FGITHHTQRG HIARATLEAV CFQTKAILEA MERDSGQTLS
DLAVDGGLSN SDICMQSQAN IIRIPVERPP MHEVTALGAA IAAGLAVGVW RNLDELVGMN
KSNRTVFEAQ ISEAESARMY KQWSKAVRMS RGWLESDEID AI
//
