ID L8ESW9_STRR1 Unreviewed; 513 AA.
AC L8ESW9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:QST80081.1};
GN ORFNames=SRIM_007725 {ECO:0000313|EMBL:QST80081.1};
OS Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS 4667 / NRRL 2234).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1265868 {ECO:0000313|EMBL:QST80081.1, ECO:0000313|Proteomes:UP000011074};
RN [1] {ECO:0000313|EMBL:QST80081.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST80081.1};
RA Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Tze-Tze L., Chu J.,
RA Guo M., Kirby R., Hoskisson P.A., Herron P.R., Hunter I.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QST80081.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST80081.1};
RA Algora L., Schniete J.K., MacFadyen A., Hoskisson P.A., Hunter I.S.,
RA Herron P.R.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QST80081.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST80081.1};
RA Algora-Gallardo L., Schniete J.K., Mark D.R., Hunter I.S., Herron P.R.;
RT "Bilateral symmetry of linear streptomycete chromosomes.";
RL bioRxiv 0:0-0(2021).
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}.
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DR EMBL; CP048261; QST80081.1; -; Genomic_DNA.
DR RefSeq; WP_003981590.1; NZ_CP048261.1.
DR AlphaFoldDB; L8ESW9; -.
DR GeneID; 66853811; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000011074; 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; cd07789; FGGY_CsGK_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: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; 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};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
KW ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 16..263
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 274..462
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT BINDING 23
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 23
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 27
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 93
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 93
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 94
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 94
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 145
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 145
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 256
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 256
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 257
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 278
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 322
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 423
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 427
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ SEQUENCE 513 AA; 55987 MW; A639D1C1D6B8F421 CRC64;
MSDNHSTASH GHGPFIAAID QGTTSSRCIV FDKDGRIVSV DQKEHEQIFP KPGWVEHDAK
EIWENVQQVV AGAVEKAGIT AKDVKAIGIT NQRETTLMWD KNTGEPVHNA IVWQDTRTDG
LCRELGRNVG KDRFRRETGL PLASYFAGPK IRWLLDNVEG LRERAEAGDI LFGTMDSWVI
WNLTGGTEGG VHVTDVTNAS RTLLMNLRKL EWDEKILHSI DIPAAVLPEI RSSAEVYGTA
ASGALAGVPV ASALGDQQAA LFGQTCYDKG EAKSTYGTGT FMLMNTGDEP VNSYNGLLTT
VGYRIGDQAP VYALEGSIAV TGSLVQWMRD QMGLINSAAE IETLASTVED NGGAYFVPAF
SGLFAPYWRS DARGVIAGLT RYVTKAHIAR AVLEATAWQT REITDAMTKD SGVDLTSLKV
DGGMTSNNLL MQTISDFLDA PVVRPMVAET TCLGAAYAAG LAVGFWPDTD ALRANWRRAA
EWTPRMDAET RDREYKNWLK AVERTMGWID DES
//
