ID A0A0B7MUD9_9FUNG Unreviewed; 854 AA.
AC A0A0B7MUD9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Name=PARPA_03222.1 scaffold 7241 {ECO:0000313|EMBL:CEP09671.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP09671.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP09671.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP09671.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU003733}.
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DR EMBL; LN722188; CEP09671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7MUD9; -.
DR STRING; 35722.A0A0B7MUD9; -.
DR OrthoDB; 2734344at2759; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
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:0098771; P:inorganic ion homeostasis; IEA:UniProt.
DR GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR NCBIfam; TIGR01297; CDF; 1.
DR NCBIfam; TIGR01311; glycerol_kin; 1.
DR PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF160240; Cation efflux protein cytoplasmic domain-like; 1.
DR SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Transferase {ECO:0000256|RuleBase:RU003733};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 51..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..593
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 603..792
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 854 AA; 93707 MW; 3BB8D18810E6935F CRC64;
MSNSVQNLER EPLLNTQVTG GSVVSYTVTQ QNCSNVTLKD RTAAQSTKRK LWFAVCLACC
FFATELVAGY FANSLALMSD AFHLLSDVAS FIVALAAIYL AEKPATKRHT FGFHRAEVIA
ALVSVLTIWV LTGFLVHEAI QRIRNPQVIN AKLMCITAAI GVLVNVILAY VLGGHHHGHS
HDEEVHVHIE NESGNQPHKE TNINLRAAAL HVLGDLLASV GKNGYSLAVL MEGVPGNIHP
DLIEKSLLDV PGVIAVHDLH VWTLSPGKYS LTAHITIDHN SSNYDEVLSK GQHIVCDVYG
VHHSTLQIES EQSLFTSHCN PELCAVRAMT QNQFIGAIDQ GTTSTRFVIF NEEGELVTWH
QMEFEQHYPH PGWVEHDPYD ILASVDTCIE HAVRKLGLMG YDASDIKCVG ITNQRETTVA
WDSKTGEPLC PAIVWSDNRT SHTVQDLANQ AHLPKEQQGI EALREICGLP ITTYFSAVKM
KWMLDHVPEV KEAHKNNRLQ FGTIDTWLIY NLTGGADKDG VLVTDVTNAS RTMLMDINTL
EWSEKAIDFF GFGGLSLAKI VPSSTVYGKI SSGSLQNVPI SGCLGDQQSA LVGQKCFRTG
DAKNTYGTGC FMLFNVGEKP VFSNNGLLST VAYQFGGQPP MYALEGSVAV AGSSIQWLRD
NMGIIQNAQQ IGELAAKVKS TAGVYFVTAF SGLFAPYWRD DARGTICGLT QFTKREHIAR
ATLEAVCYQT RAILEAMDKD AKQPLRSLKV DGGVSNSDIC MQIQADLLNI EVHRPKMRET
TALGAAIAAG LATGIWKSTD DLQQVNEDGR AIFKSQISDK KREKMYNGWK EAIQRSLGWA
QVLGQTSDTD DEDY
//
