ID A0A1S8CSS2_9GAMM Unreviewed; 495 AA.
AC A0A1S8CSS2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-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=BKE30_12600 {ECO:0000313|EMBL:ONG38346.1};
OS Alkanindiges hydrocarboniclasticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Alkanindiges.
OX NCBI_TaxID=1907941 {ECO:0000313|EMBL:ONG38346.1, ECO:0000313|Proteomes:UP000192132};
RN [1] {ECO:0000313|EMBL:ONG38346.1, ECO:0000313|Proteomes:UP000192132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:ONG38346.1,
RC ECO:0000313|Proteomes:UP000192132};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Alkanindiges sp. strain H1.";
RL Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00186}.
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:ONG38346.1}.
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; MLCN01000034; ONG38346.1; -; Genomic_DNA.
DR RefSeq; WP_076878959.1; NZ_MLCN01000034.1.
DR AlphaFoldDB; A0A1S8CSS2; -.
DR STRING; 1907941.BKE30_12600; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000192132; 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 CDD; cd07786; FGGY_EcGK_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; PS00933; FGGY_KINASES_1; 1.
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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00186};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00186}.
FT DOMAIN 3..249
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 259..447
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 242..243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT BINDING 409..413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ SEQUENCE 495 AA; 54435 MW; 1CA0FA73E066FF09 CRC64;
MDYLLALDQG TTSSRAIIFD SKGQIKASAQ REITIRTPHP GWVEQDAQEL WNTQIGVAQQ
AMAAAGLLAQ DIAAIGLTNQ RETTVVWHKK TGKPVAPAIV WQDRRTAEWC EQQRKLMDEH
KLCKKTGLRL DPYFSAGKLV WILENLPEAR SLANEGNLAF GTVDSWLIWN LTRGEQHVID
MSNASRTLLM NIQTQTWDKE LLDYFNIPAS ILPTIVPSGG LIGYTADGLL GRKVPICAAI
GDQQAALFGQ GCFSAGLAKN TYGTGCFMLM NTGNELKYSQ HQLLSTLAWQ TPQQQPQYAL
EGSVFMAGAI VQWLRDGLGI IRQSSEVETL ARQVKDTDGV VLVPAFTGLG APYWDSEARA
MLTGMTRGTN RCHIARAALE SIAFQVADVL VAMQQDAPAP LTELRVDGGA CCNDTLMQFQ
ADLLGVPVLR PKLQETTALG AALMAGLGVG LFSCTHDIEH LWQLDRSFEP SMNNDERQQH
LYQWHQAVSK ARTNS
//