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Database: UniProt
Entry: GLPK_RHOP2
LinkDB: GLPK_RHOP2
Original site: GLPK_RHOP2 
ID   GLPK_RHOP2              Reviewed;         501 AA.
AC   Q2IZ89;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=RPB_1763;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00186}.
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DR   EMBL; CP000250; ABD06471.1; -; Genomic_DNA.
DR   RefSeq; WP_011440659.1; NC_007778.1.
DR   AlphaFoldDB; Q2IZ89; -.
DR   SMR; Q2IZ89; -.
DR   STRING; 316058.RPB_1763; -.
DR   KEGG; rpb:RPB_1763; -.
DR   eggNOG; COG0554; Bacteria.
DR   HOGENOM; CLU_009281_2_3_5; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000008809; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
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:SF78; 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; Glycerol metabolism; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..501
FT                   /note="Glycerol kinase"
FT                   /id="PRO_1000020765"
FT   BINDING         11
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         11
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         15
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         81
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         81
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         82
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         82
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         133
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         133
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         242
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         242
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         243
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         264
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         307
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         411
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   501 AA;  54057 MW;  6CACAFB420C46D45 CRC64;
     MPFVMAIDQG TTSSRAILFR GDISIAASAQ QEFPQHFPAS GWVEHEPEDI WASTLATCRA
     AMEKAGATAA DIAAIGITNQ RETVVVWDAA SGKAIHRAIV WQDRRTAEVC TRMKADGYEP
     MITDKTGLII DPYFSGTKVA WLLDNVPGAR ARAERGELKF GTIDCWLLWR LTGGRVHATD
     ATNASRTLLF NIHTGDWDDE LLQLLRVPRS MLPEVKDSSA HFGDSAYELF GAPIAIRGIA
     GDQQAATIGQ ACFSPGMIKS TYGTGCFALL ITGATPVKSH NKLLTTIAYQ LGGKRTYALE
     GSIFVAGSAV QWLRDGLGII KHASETGPLA DKSDSMQSVY LVPAFVGLGA PYWNPRVRGA
     LFGMTRNTGP AELAHAALES VCYQTYDLWA AMRADWSGAD AAPPVLRVDG GMAASDWTMQ
     RLADLLDAPV DRPVIQETTA LGAAYLAGLS AGVFPEPQKF ADNWRLDHRF RPAMSQATRE
     RKLAGWGRAV KGLLASDEGE G
//
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