ID A0A238ZTS9_9PSEU Unreviewed; 506 AA.
AC A0A238ZTS9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN06265360_12536 {ECO:0000313|EMBL:SNR86836.1};
OS Haloechinothrix alba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Haloechinothrix.
OX NCBI_TaxID=664784 {ECO:0000313|EMBL:SNR86836.1, ECO:0000313|Proteomes:UP000198348};
RN [1] {ECO:0000313|EMBL:SNR86836.1, ECO:0000313|Proteomes:UP000198348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45207 {ECO:0000313|EMBL:SNR86836.1,
RC ECO:0000313|Proteomes:UP000198348};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZNW01000025; SNR86836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238ZTS9; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000198348; 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:UP000198348};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
KW ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 5..256
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 266..455
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT BINDING 12
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 12
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 16
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 82
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 82
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 83
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 83
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 134
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 134
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 249
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 249
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 250
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 271
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 315
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 416
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 420
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ SEQUENCE 506 AA; 55513 MW; EA34D640681D3259 CRC64;
MSEFIGSIDQ GTTSTRFMVF DHGGNEIVRH QLEHEQILPR AGWVEHNPTE IWERTRSVIT
TAMNKADLGA GDLAAVGITN QRETTVVWNR RTGRTYCNAI VWQDTRTDKI ANALHRDGRA
EVVRQRSGLP PATYFAGGKL KWILDNVEGV RADAEKGEAI FGTIDTWLLW NLTGGTDGGV
HATDATNASR TMLMDLETWD WDDELLSFFD VPRKMLPFIL PSSNPEFYGT TRADGPFGGE
VPLTGVLGDQ QAATVGQVCF KPGEAKNTYG TGNFLLLNTG NEIVRSEHGL LTTICYQFGE
HKPVYALEGS IAVTGSAVQW LRDQLGIISG AAQSEALAGQ VSDNGGVYFV PAFSGLFAPY
WRSDARGAIV GLSRYSTNAH IARATLESIC FQTRDVVDAM QADSGVTLDV LRADGGVTAN
ELCMQMQADV LGVPVYRPVV AETTALGAAY AAGLAVGFWR STDELVENWQ EDKRWQPTWD
SDRRESEHAR WKKAVSRTLD WVDVDG
//
