ID A0A367LQ20_9HYPO Unreviewed; 555 AA.
AC A0A367LQ20;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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};
DE Flags: Fragment;
GN ORFNames=L249_2784 {ECO:0000313|EMBL:RCI16554.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI16554.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI16554.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI16554.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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:RCI16554.1}.
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DR EMBL; LKCN02000001; RCI16554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LQ20; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000253664; Unassembled WGS sequence.
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; IPR000577; Carb_kinase_FGGY.
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; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|RuleBase:RU003733};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..555
FT /note="glycerol kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016835502"
FT DOMAIN 72..303
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 314..503
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RCI16554.1"
SQ SEQUENCE 555 AA; 59565 MW; 18E0F339973BD50F CRC64;
AHFGFLWLLA AAHDTIVSSS LPLDFSLQGK NDGRQDPGQR RRKRLCWEHR SGHDLDPFSY
LQSGRRARCW SSSPICSKHP QPGWHEHDPL ELLRSVETCI QHAVSDFRAS GHHTAQIRAI
GLANQRETLV AWDTATGEPL CDAVVWSDTR TAPLVRELKA RDGADVLVHR CGQPPSTSAS
AIKLLWLLCH VEAVARAYDA GRLAVGTVDT WLIYRLNGGV RRPGGPIYVT DSTNASRTMW
MDIRTRQYDH ELLSFFGVDR AKLTLPTIVS SSHPTAFGAL AYGPLAGTRI AACLGDQSAA
LVGHGGFSPG KAKSTYGTGC FLLYNVGPEP VISKNGLQAT VAYDLGDGRP PAYALEGSVS
VAGSGINFLV NNLDFVDSHK AIDHLALSVP DNGGVYFVTA FSGLLAPYWI DDAQGTLFGL
TAHTQKGHIA RATLEAVCHQ TAAILDAMAA DSGHALDSLA VDGGLAGSDV CMQTQADLSG
IPVDRPCMRE ATSLGAALAA GLATGVWDGL DQLVHVGTSG RSLFRPGIVK EERCARRRRW
ARAVEMSRGW LAEVA
//