GLPK_MYCTA
ID GLPK_MYCTA Reviewed; 517 AA.
AC A5U920;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=MRA_3731;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_00186};
CC -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00186}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; CP000611; ABQ75520.1; -; Genomic_DNA.
DR RefSeq; WP_003899643.1; NC_009525.1.
DR AlphaFoldDB; A5U920; -.
DR SMR; A5U920; -.
DR STRING; 419947.MRA_3731; -.
DR EnsemblBacteria; ABQ75520; ABQ75520; MRA_3731.
DR KEGG; mra:MRA_3731; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_11; -.
DR OMA; PESGWHE; -.
DR OrthoDB; 233605at2; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_00186; Glycerol_kin; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..517
FT /note="Glycerol kinase"
FT /id="PRO_1000020748"
FT BINDING 24..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 261..262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 428..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 517 AA; 55860 MW; 7E3F30DCF2A1E63E CRC64;
MSDAILGEQL AESSDFIAAI DQGTTSTRCM IFDHHGAEVA RHQLEHEQIL PRAGWVEHNP
VEIWERTASV LISVLNATNL SPKDIAALGI TNQRETTLVW NRHTGRPYYN AIVWQDTRTD
RIASALDRDG RGNLIRRKAG LPPATYFSGG KLQWILENVD GVRAAAENGD ALFGTPDTWV
LWNLTGGPRG GVHVTDVTNA SRTMLMDLET LDWDDELLSL FSIPRAMLPE IASSAPSEPY
GVTLATGPVG GEVPITGVLG DQHAAMVGQV CLAPGEAKNT YGTGNFLLLN TGETIVRSNN
GLLTTVCYQF GNAKPVYALE GSIAVTGSAV QWLRDQLGII SGAAQSEALA RQVPDNGGMY
FVPAFSGLFA PYWRSDARGA IVGLSRFNTN AHLARATLEA ICYQSRDVVD AMEADSGVRL
QVLKVDGGIT GNDLCMQIQA DVLGVDVVRP VVAETTALGV AYAAGLAVGF WAAPSDLRAN
WREDKRWTPT WDDDERAAGY AGWRKAVQRT LDWVDVS
