ID G2GBQ7_9ACTN Unreviewed; 513 AA.
AC G2GBQ7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ORFNames=SZN_14656 {ECO:0000313|EMBL:EGX59080.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX59080.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX59080.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX59080.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX59080.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGBF01000038; EGX59080.1; -; Genomic_DNA.
DR RefSeq; WP_007495601.1; NZ_AGBF01000038.1.
DR AlphaFoldDB; G2GBQ7; -.
DR PATRIC; fig|700597.3.peg.2871; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000004217; Unassembled WGS sequence.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000004217};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
KW ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 11..262
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 274..461
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT BINDING 18
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 18
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 22
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 88
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 88
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 89
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 89
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 140
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 140
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 255
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 255
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 277
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 321
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 422
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 426
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ SEQUENCE 513 AA; 55980 MW; 4C6EE60B97C7C41C CRC64;
MTDAHTAGPF IAAIDQGTTS SRCIVFDRDG RIVAVDQKEH EQIFPKPGWV EHDATEIWTN
VQEVVAGAVA KAGITRDDIK AIGITNQRET TVLWDKNTGE PVHHAIVWQD TRTDALCREL
GRNVGQDRFR RETGLPLASY FAGPKARWLL DNVEGLKERA EAGDILFGTM DTWVIWNLTG
GVDGGRHVTD VTNASRTMLM NLHTMEWDEK IAESIGVPLQ LLPEIRSSAE VYGEITGGEL
GELLGGIPVA SALGDQQAAL FGQTCFAEGE TKSTYGTGTF MVMNTGDKII NSYAGLLTTV
GYKIGDQDTV YALEGSIAVT GSLVQWMRDQ MGLISTAAEI ETLALSVEDN GGAYFVPAFS
GLFAPHWRSD ARGVIAGLTR YVTKAHLARA VLEATAWQTR EIADAMTKDS GVELATLKVD
GGMTANNLLM QTLSDVLDAP VVRPMVAETT CLGAAYAAGL AVGFWTSTDE LRANWRRAAE
WTPRMDAETR DREYKNWLKA VERTMGWLED DEN
//
