ID A9HHY3_GLUDA Unreviewed; 499 AA.
AC A9HHY3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 112.
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 ECO:0000313|EMBL:CAP55696.1};
GN OrderedLocusNames=GDI1753 {ECO:0000313|EMBL:CAP55696.1};
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP55696.1, ECO:0000313|Proteomes:UP000001176};
RN [1] {ECO:0000313|EMBL:CAP55696.1, ECO:0000313|Proteomes:UP000001176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC PAl5 {ECO:0000313|Proteomes:UP000001176};
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
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|HAMAP-Rule:MF_00186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
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|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|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; AM889285; CAP55696.1; -; Genomic_DNA.
DR RefSeq; WP_012225263.1; NC_011365.1.
DR STRING; 272568.GDI1753; -.
DR KEGG; gdi:GDI1753; -.
DR KEGG; gdj:Gdia_3533; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_5; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001176; Chromosome.
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-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07786; FGGY_EcGK_like; 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 PANTHER; PTHR10196:SF78; 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|HAMAP-Rule:MF_00186, ECO:0000256|RuleBase:RU003733};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00186}; Reference proteome {ECO:0000313|Proteomes:UP000001176};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
KW ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 7..251
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 261..449
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT BINDING 14
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
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 14
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 18
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
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 244
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 244
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 266
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 309
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 410
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 414
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ SEQUENCE 499 AA; 53842 MW; 32DFE2A24B0DF1F1 CRC64;
MNKKTTILAI DQGTTSTRSI IFDRDATPLA TSRIEFAQHY PDHGWVEHDA EEIWRDALST
ARAAIEQGGG VDAIAALGIT NQRETIVVWD RATGTPIHRA IVWQDRRTAS MCARMRQDGC
EGLVRDRTGL LLDPYFSASK LAWMLDNVPG ARASAEAGRL AFGTIDSFLL WRLTGGRVHA
TDVTNASRTL LFDIHRQVWD DDLLRLFGIP AALLPEVRGN SEIYGETDPA LFGRPIPVAG
MAGDQQAALV GQACFAPGMA KATYGTGCFV LLNTGTAPVQ SANRMLTTIG YRIGDRTTYA
LEGAIFVAGA AIKWLRDGLH LITHASQTDD MATRIPHSHG VYMVPGFVGL GAPHWDPEAR
GLICGLTLDA TAAHIARAAL ESVAYQTYDL MAAMAQDGGG AVTTLRVDGG MAANDWFCRF
LSDVLQARVE RPRHLETTAT GAAFLAGLAT GVWTDLDDVA ARRARGSLFQ PTMDLAQRGT
MLDGWHQAVR RTLTADASA
//
