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

 A0A0R1PV93_9LACO        Unreviewed;       502 AA.
A0A0R1PV93;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
27-SEP-2017, entry version 12.
RecName: Full=Glycerol kinase {ECO:0000256|HAMAP-Rule:MF_00186};
EC=2.7.1.30 {ECO:0000256|HAMAP-Rule:MF_00186};
AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00186};
AltName: Full=Glycerokinase {ECO:0000256|HAMAP-Rule:MF_00186};
Short=GK {ECO:0000256|HAMAP-Rule:MF_00186};
Name=glpK {ECO:0000256|HAMAP-Rule:MF_00186};
ORFNames=FD33_GL002180 {ECO:0000313|EMBL:KRL32611.1};
Lactobacillus paralimentarius DSM 13238 = JCM 10415.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
Lactobacillus.
NCBI_TaxID=1122151 {ECO:0000313|EMBL:KRL32611.1, ECO:0000313|Proteomes:UP000051908};
[1] {ECO:0000313|EMBL:KRL32611.1, ECO:0000313|Proteomes:UP000051908}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 13238 {ECO:0000313|EMBL:KRL32611.1,
ECO:0000313|Proteomes:UP000051908};
PubMed=26415554; DOI=10.1038/ncomms9322;
Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
"Expanding the biotechnology potential of lactobacilli through
comparative genomics of 213 strains and associated genera.";
Nat. Commun. 6:8322-8322(2015).
-!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
glycerol 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|SAAS:SAAS00193194}.
-!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
phosphate. {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|SAAS:SAAS00029899}.
-!- ENZYME REGULATION: Activated by phosphorylation and inhibited by
fructose 1,6-bisphosphate (FBP). {ECO:0000256|HAMAP-
Rule:MF_00186}.
-!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_00186, ECO:0000256|SAAS:SAAS00030105}.
-!- SUBUNIT: Homotetramer and homodimer (in equilibrium).
{ECO:0000256|HAMAP-Rule:MF_00186}.
-!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase
system (PTS), including enzyme I, and histidine-containing protein
(HPr) are required for the phosphorylation, which leads to the
activation of the enzyme. {ECO:0000256|HAMAP-Rule:MF_00186}.
-!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
Rule:MF_00186, ECO:0000256|RuleBase:RU003733,
ECO:0000256|SAAS:SAAS00546148}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KRL32611.1}.
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EMBL; AZES01000003; KRL32611.1; -; Genomic_DNA.
RefSeq; WP_025086004.1; NZ_BAMH01000084.1.
EnsemblBacteria; KRL32611; KRL32611; FD33_GL002180.
PATRIC; fig|1122151.5.peg.2252; -.
UniPathway; UPA00618; UER00672.
Proteomes; UP000051908; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|SAAS:SAAS00082951};
Complete proteome {ECO:0000313|Proteomes:UP000051908};
Glycerol metabolism {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|SAAS:SAAS00029437};
Kinase {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777,
ECO:0000313|EMBL:KRL32611.1};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|SAAS:SAAS00082951};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00186};
Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777,
ECO:0000313|EMBL:KRL32611.1}.
DOMAIN 5 252 FGGY_N. {ECO:0000259|Pfam:PF00370}.
DOMAIN 262 450 FGGY_C. {ECO:0000259|Pfam:PF02782}.
NP_BIND 13 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
NP_BIND 411 415 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
REGION 83 84 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00186}.
REGION 245 246 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00186}.
BINDING 13 13 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00186}.
BINDING 17 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
BINDING 135 135 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00186}.
BINDING 267 267 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
BINDING 310 310 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00186}.
BINDING 314 314 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00186}.
BINDING 329 329 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
MOD_RES 231 231 Phosphohistidine; by HPr.
{ECO:0000256|HAMAP-Rule:MF_00186}.
SEQUENCE 502 AA; 55869 MW; FC68873E9F1656E2 CRC64;
MSNEYIMAID EGTTSTRAII FDQKGNKIAD AQREFTQYFP EPGWVEHDAN EIWNAVQSTI
ANVFIESGIK PDQIKGIGIT NQRETTVVWD KTTGLPIYNA IVWQSRQTTD IAEKLAGRGY
GEMIHEKTGL LIDPYFSATK IRWILDHVKG AQKRAEDGEL LFGTIDSWLL WKLSGGAAHI
TDYSNASRTM LFNIHSLEWD KDILRILNIP QAMLPEVRPN SEVYAKTKDY HFYGSEVPIA
GMIGDQQAAL FGQMAFEPGM VKNTYGTGAF IVMNTGEKPQ LSDNNLLTTI GYGINNKIYY
ALEGSIFVAG SAIQWLRDAM NLVDSAPQSE EAALASTDQD EVYVVPAFTG LGAPYWDADA
RGAVFGLTRG TTKNDFIKAT LQSLAYQSRD VLDTMKKDTG IDIPTLKVDG GAANNRYLMQ
FQADILQTPV QRAKDLETTA LGAAFLAGLA VGYWDNLYDI KKQYATGATF EPEMDQEHAD
YLYEGWREAV SATRKFKHKT TK


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