GLPK_PYRFU
ID GLPK_PYRFU Reviewed; 490 AA.
AC Q8TZI8;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PF2004;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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 -!- 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; AE009950; AAL82128.1; -; Genomic_DNA.
DR RefSeq; WP_011013149.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TZI8; -.
DR SMR; Q8TZI8; -.
DR STRING; 186497.PF2004; -.
DR EnsemblBacteria; AAL82128; AAL82128; PF2004.
DR GeneID; 41713830; -.
DR KEGG; pfu:PF2004; -.
DR PATRIC; fig|186497.12.peg.2081; -.
DR eggNOG; arCOG00024; Archaea.
DR HOGENOM; CLU_009281_2_3_2; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 25345at2157; -.
DR PhylomeDB; Q8TZI8; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001013; 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 HAMAP; MF_00186; Glycerol_kin; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
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;
KW Reference proteome; Transferase.
FT CHAIN 1..490
FT /note="Glycerol kinase"
FT /id="PRO_0000059529"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 400..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 490 AA; 55046 MW; 60A0BBB0EE297A3F CRC64;
MDRYILSLDE GTTSARAIIF DKNSNVLGIG QYEFPQYYPK PGWVEHNPEE IWEAQVKAIK
TAIEKAKIEA NQIAAIGVTN QRETTVIWKK DGKPVYNAIV WQCRRTAEMV EEIKREYSDV
IKEKTGLVPD AYFSASKIAW LLDNVPGLRE KAEKGEVMFG TIDTFLIYRL TGEHVTDYSN
ASRTMLFNIN KLEWDEELLE IFKIPDGILP DVKESSEIYG YTKILGPEIP VSGDAGDQQA
ALFGQAAFEE GMVKATYGTG NFILANTGRM LLYSDNLLTT VAWGINGKVN YALEGSIFIT
GAAVQWLRDG IKIISNAAET EELATKLESN EGVYFVPAFV GLGAPYWDQF ARGLIIGITR
GTGREHLARA TLEAIAYLTR DVIEEMEKLI QIKELRVDGG ATVNNFLMQF QADILNKKVI
RPVVKETTAL GAAYLAGLAV DYWESMEEIS QLWRAERVFE PQMDEKTREK LYRGWKEAVK
RALGWAKVVS
