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Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK)

 GLPK_SALPB              Reviewed;         502 AA.
A9MZH4;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 1.
07-JUN-2017, entry version 58.
RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186};
OrderedLocusNames=SPAB_05061;
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=1016998;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-1250 / SPB7;
The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
Nash W., Johnson M., Thiruvilangam P., Wilson R.;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}.
-!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}.
-!- ENZYME REGULATION: Activity of this regulatory enzyme is affected
by several metabolites. Allosterically and non-competitively
inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated
phosphocarrier protein EIIA-Glc (III-Glc), an integral component
of the bacterial phosphotransferase (PTS) system.
{ECO:0000255|HAMAP-Rule:MF_00186}.
-!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_00186}.
-!- SUBUNIT: Homotetramer and homodimer (in equilibrium). Heterodimer
with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc
dimer. The zinc ion is important for dimerization.
{ECO:0000255|HAMAP-Rule:MF_00186}.
-!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
Rule:MF_00186}.
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EMBL; CP000886; ABX70352.1; -; Genomic_DNA.
RefSeq; WP_000136809.1; NC_010102.1.
ProteinModelPortal; A9MZH4; -.
SMR; A9MZH4; -.
EnsemblBacteria; ABX70352; ABX70352; SPAB_05061.
KEGG; spq:SPAB_05061; -.
PATRIC; fig|1016998.12.peg.4750; -.
HOGENOM; HOG000222134; -.
KO; K00864; -.
OMA; WQDTRTQ; -.
UniPathway; UPA00618; UER00672.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_00186; Glycerol_kin; 1.
InterPro; IPR000577; Carb_kinase_FGGY.
InterPro; IPR018485; Carb_kinase_FGGY_C.
InterPro; IPR018483; Carb_kinase_FGGY_CS.
InterPro; IPR018484; Carb_kinase_FGGY_N.
InterPro; IPR005999; Glycerol_kin.
Pfam; PF02782; FGGY_C; 1.
Pfam; PF00370; FGGY_N; 1.
PIRSF; PIRSF000538; GlpK; 1.
TIGRFAMs; TIGR01311; glycerol_kin; 1.
PROSITE; PS00933; FGGY_KINASES_1; 1.
PROSITE; PS00445; FGGY_KINASES_2; 1.
3: Inferred from homology;
Allosteric enzyme; ATP-binding; Glycerol metabolism; Kinase;
Metal-binding; Nucleotide-binding; Transferase; Zinc.
CHAIN 1 502 Glycerol kinase.
/FTId=PRO_1000077427.
NP_BIND 14 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
NP_BIND 412 416 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
REGION 84 85 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00186}.
REGION 234 236 Allosteric FBP inhibitor binding.
REGION 246 247 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00186}.
METAL 479 479 Zinc; shared with EIIA-Glc.
{ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 14 14 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00186}.
BINDING 18 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 136 136 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00186}.
BINDING 268 268 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 311 311 ATP; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 315 315 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 330 330 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
SEQUENCE 502 AA; 56052 MW; A780A522CA16C1B4 CRC64;
MTEKKYIVAL DQGTTSSRAV VMDHDANIVS VSQREFEQIY PKPGWVEHDP MEIWASQSST
LVEVLAKADI SSDQIAAIGI TNQRETAIVW ERETGKPIYN AIVWQCRRTA DICEQLKRDG
LEDYIRDNTG LVVDPYFSGT KVKWILDHVE GSRERAKRGE LLFGTVDTWL IWKMTQGRVH
VTDYTNASRT MLFNIHDLDW DDKMLDVLDI PRAMLPQVRK SSEVYGQTNI GGKGGTRIPI
AGIAGDQQAA LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPSGEVN
YALEGAVFMA GASIQWLRDE MKLISDAFDS EYFATKVKDT NGVYVVPAFT GLGAPYWDPY
ARGAIFGLTR GVNSNHIIRA TLESIAYQTR DVLEAMQADS GIRLHALRVD GGAVANNFLM
QFQSDILGTR VERPEVREVT ALGAAYLAGL AVGYWQNLDE LQEKAVIERE FRPGIETTER
NYRYSGWKKA VKRAMAWEEH DK


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