GLPK_HALVD
ID GLPK_HALVD Reviewed; 510 AA.
AC D4GYI5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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};
GN Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=HVO_1541;
GN ORFNames=C498_03060;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=DS2 / DS70;
RX PubMed=19411322; DOI=10.1128/jb.00131-09;
RA Sherwood K.E., Cano D.J., Maupin-Furlow J.A.;
RT "Glycerol-mediated repression of glucose metabolism and glycerol kinase as
RT the sole route of glycerol catabolism in the haloarchaeon Haloferax
RT volcanii.";
RL J. Bacteriol. 191:4307-4315(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=24379808; DOI=10.3389/fmicb.2013.00376;
RA Ouellette M., Makkay A.M., Papke R.T.;
RT "Dihydroxyacetone metabolism in Haloferax volcanii.";
RL Front. Microbiol. 4:376-376(2013).
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. It also catalyzes the phosphorylation of
CC dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM,
CC in the metabolism of DHA. {ECO:0000255|HAMAP-Rule:MF_00186,
CC ECO:0000269|PubMed:19411322, ECO:0000269|PubMed:24379808}.
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 -!- INDUCTION: By glycerol. Not subjected to glucose catabolite repression.
CC {ECO:0000269|PubMed:19411322}.
CC -!- DISRUPTION PHENOTYPE: Incapable of growth on glycerol. Causes a
CC reduction in growth on dihydroxyacetone. {ECO:0000269|PubMed:19411322,
CC ECO:0000269|PubMed:24379808}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; CP001956; ADE04400.1; -; Genomic_DNA.
DR EMBL; AOHU01000028; ELY35766.1; -; Genomic_DNA.
DR RefSeq; WP_004041419.1; NZ_AOHU01000028.1.
DR AlphaFoldDB; D4GYI5; -.
DR SMR; D4GYI5; -.
DR STRING; 309800.C498_03060; -.
DR EnsemblBacteria; ADE04400; ADE04400; HVO_1541.
DR EnsemblBacteria; ELY35766; ELY35766; C498_03060.
DR GeneID; 8926676; -.
DR KEGG; hvo:HVO_1541; -.
DR PATRIC; fig|309800.29.peg.590; -.
DR eggNOG; arCOG00024; Archaea.
DR HOGENOM; CLU_009281_2_3_2; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 25345at2157; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; 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 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; PS00445; FGGY_KINASES_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..510
FT /note="Glycerol kinase"
FT /id="PRO_0000428947"
FT BINDING 14..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 84..85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 422..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 510 AA; 56737 MW; 54C784AEE8B3552C CRC64;
MSGETYVGAI DQGTTGTRFM VFDHDGKVVA NAYEKHEQIY PEPGWVEHDA NEIWDNTKQV
IDAALSSAGL DAEQLEAIGI TNQRETTLVW DRETGQPIHN AIVWQDRRTT DRIETLEAEG
KTDDVRAKTG LEPDAYFSAT KAEWLLDNSD PIKLQRSRPE DIRDRAADGE LAFGTIDTWL
IYNLTGNHIT DVTNASRTML FNIHDMEWDD ELLDEFNVPR ELLPEVRPSS DDDYYGTTDA
DGFLGAEVPV AGALGDQQAA LFGQTCFDAG DAKNTYGTGS FMLMNTGDEA VMSEHGLLTT
VGFQRSGEPV QYALEGSIFI TGAAIEWLED MTLIDNAAES EKLARSVEST DGVYFVPAFT
GLGAPHWDQR ARGTIVGMTR GTRREHIVRA TLESIAFQTR DVAEAMESDS EIDLSSLRVD
GGAVKNNFLC QLQSNILDTE IVRPQVDETT ALGAAYAAGL AVGYWETLDE LRENWQVDRE
FAPKDPQNVE HRYGRWKEAV DRSLDWAREE
