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Database: UniProt
Entry: A0A2U2RX33_9BACT
LinkDB: A0A2U2RX33_9BACT
Original site: A0A2U2RX33_9BACT 
ID   A0A2U2RX33_9BACT        Unreviewed;       497 AA.
AC   A0A2U2RX33;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:PWH10400.1};
GN   ORFNames=DEJ39_06515 {ECO:0000313|EMBL:PWH10400.1};
OS   Bacteroidetes bacterium SCGC AAA795-G10.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=2175803 {ECO:0000313|EMBL:PWH10400.1, ECO:0000313|Proteomes:UP000246014};
RN   [1] {ECO:0000313|EMBL:PWH10400.1, ECO:0000313|Proteomes:UP000246014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AAA795-G10 {ECO:0000313|EMBL:PWH10400.1};
RA   Ngugi D.K., Stingl U.;
RT   "High-quality draft single-cell genome of the NS5 marine group from the
RT   coastal Red Sea.";
RL   Submitted (MAY-2018) 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:PWH10400.1}.
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DR   EMBL; QFDA01000004; PWH10400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2RX33; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000246014; 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}; Reference proteome {ECO:0000313|Proteomes:UP000246014};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00186}.
FT   DOMAIN          4..250
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          260..448
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   BINDING         12..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         243..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         265
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   497 AA;  55083 MW;  E31F1D2DDD090665 CRC64;
     MSEYILSIDA GTTSSRAIIF DKKGKTIGVS QHEFTQFFPK EGWVEHDALE IWNTQLKAIK
     EVLQKTNIDA SQINALGITN QRETTLLWDR NTGVPVHKAI VWQDRRTTNI CNSILKEGKA
     DLFYEKTGLI LDSYFSGTKI KWILDQDPDL RKKADNGEII FGTIDSWLIW NLTGGKVHVT
     DVTNASRTLL FNIRSLKWDS ELLEILDIPE KILPKIVSCS EKIAYTTEGL FEDKILISGI
     AGDQQAALFG QMCINPGDVK NTYGTGCFCI MNTGDKPVKS KNRMLTTIGY RINNKTQYAL
     EGSVFVAGAA VQWLRDQLGI ISSASEIESL AKTVKNNGGV TFIPALSGLA APYWDPHATG
     TITGITRGTQ KGHIARATLE AIAMRTKEII TAMEKDAKFK FKSLKVDGGA SNNDLLMQIQ
     SNLLGVNVIR PKTTETTALG AAFFAGLASG FWSSLEKLSS VWNIDKEFNP KENEETLSIV
     NNWEKRILKM SNSQNNE
//
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