ID   Q1AX49_RUBXD            Unreviewed;       503 AA.
AC   Q1AX49;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   10-JUN-2026, entry version 128.
DE   RecName: Full=Glycerol kinase {ECO:0000256|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000256|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000256|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000256|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000256|HAMAP-Rule:MF_00186};
GN   OrderedLocusNames=Rxyl_1063 {ECO:0000313|EMBL:ABG04029.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / JCM 11954 / NBRC 16129 /
OS   PRD-1).
OC   Bacteria; Bacillati; Actinomycetota; Rubrobacteria; Rubrobacterales;
OC   Rubrobacteraceae; Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04029.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG04029.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
CC       glycerol 3-phosphate. {ECO:0000256|ARBA:ARBA00054633,
CC       ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + ATP = sn-glycerol 3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000256|ARBA:ARBA00052101,
CC         ECO:0000256|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {ECO:0000256|HAMAP-Rule:MF_00186}.
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, ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|HAMAP-Rule:MF_00186,
CC       ECO:0000256|RuleBase:RU003733}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00186}.
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DR   EMBL; CP000386; ABG04029.1; -; Genomic_DNA.
DR   RefSeq; WP_011564047.1; NC_008148.1.
DR   AlphaFoldDB; Q1AX49; -.
DR   STRING; 266117.Rxyl_1063; -.
DR   KEGG; rxy:Rxyl_1063; -.
DR   eggNOG; COG0554; Bacteria.
DR   HOGENOM; CLU_009281_2_3_11; -.
DR   OrthoDB; 9805576at2; -.
DR   PhylomeDB; Q1AX49; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000006637; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd07786; FGGY_EcGK_like; 1.
DR   FunFam; 3.30.420.40:FF:000007; Glycerol kinase; 1.
DR   FunFam; 3.30.420.40:FF:000008; Glycerol kinase; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
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   NCBIfam; NF000756; PRK00047.1; 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   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, ECO:0000256|HAMAP-
KW   Rule:MF_00186};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798, ECO:0000256|HAMAP-
KW   Rule:MF_00186};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00186}; Reference proteome {ECO:0000313|Proteomes:UP000006637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00186}.
FT   DOMAIN          5..252
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          262..451
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   BINDING         13
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         13
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         83
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         83
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         84
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         84
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         135
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         135
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         245
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         245
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         246
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         267
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         412
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         416
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   503 AA;  55499 MW;  4F3ED0F1C4121F56 CRC64;
     MAGEYVLAID QGTTGTTVLI FDREGRVAGR AYSEFTQHYP RPGWVEHDPN EIWDVSMRVV
     GEALGDAKVS ARQLAAIGIT NQRETTVMWD RRTGEPVANA IVWQDRRTAG TCDRLKDEGL
     EETFRKKTGL VIDAYFSGTK VKWFLDNVAG LRERAGRGEV AFGTVDSWLV YRLTGGRAHI
     TDYSNASRTL MYNIYDLRWD EELLEILGVP EGVLPEVKPS SHVYGETDPG AFFQASVPVA
     GIAGDQQAAL FGQAAYERGL AKNTYGTGSF VLMNTGNEAV PSKEGLLTTI AWGIGEEPVE
     YALEGAIFIT GAAVQWLRDG LGIIRSAAET EELAKSVQSN DGVYFVPALV GLGAPHWDAY
     ARGTIVGITR GTTKAHLARA ALESMCYQTL DVVRAMERDS GIELKELRAD GGAVANSFLM
     QFQSDILGVP VEVPEITETT ALGSAYLAGL ATGFWESREE LDARWRLSRR YEPSMQEGER
     ERLHRRWLRA VERSRGWDRE EEG
//