GenomeNet

Database: UniProt
Entry: A0A1S8CSS2_9GAMM
LinkDB: A0A1S8CSS2_9GAMM
Original site: A0A1S8CSS2_9GAMM 
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
//
DBGET integrated database retrieval system