GLPK2_SULAC
ID GLPK2_SULAC Reviewed; 497 AA.
AC Q4J7A3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Glycerol kinase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=Glycerokinase 2 {ECO:0000255|HAMAP-Rule:MF_00186};
DE Short=GK 2 {ECO:0000255|HAMAP-Rule:MF_00186};
GN Name=glpK2 {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=Saci_2033;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY81329.1; -; Genomic_DNA.
DR RefSeq; WP_011278831.1; NC_007181.1.
DR AlphaFoldDB; Q4J7A3; -.
DR SMR; Q4J7A3; -.
DR STRING; 330779.Saci_2033; -.
DR EnsemblBacteria; AAY81329; AAY81329; Saci_2033.
DR GeneID; 3474450; -.
DR KEGG; sai:Saci_2033; -.
DR PATRIC; fig|330779.12.peg.2032; -.
DR eggNOG; arCOG00024; Archaea.
DR HOGENOM; CLU_009281_2_3_2; -.
DR OMA; FMLMNIG; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001018; 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..497
FT /note="Glycerol kinase 2"
FT /id="PRO_0000059532"
FT BINDING 13..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 241..242
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 263
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 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 406..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 497 AA; 55356 MW; 8AEF78EEEF675CEB CRC64;
MAEKYVIAID EGTTSARAIV FDKELNILGI GQNEFTQYYP QPGYVEHSPE EIWQAQLLAI
NKALEKAKID RNNILSIGIT NQRETTVMWD TRTGKPIYNA IVWQDRRTAP ITDYLKANYL
RLIKDRTGLV PDPYFSASKI KWILDNIPNA REKAEKGEIK FGTIDTYLIW KLTNGKAHVT
DYSNASRTML FNIRKLEWDR EILEILNIPE AILPDVKPSS EIYGYAEILN SSIPISGDAG
DQQAALFGQI AFNQGDVKCT YGTGSFILLN TGSNLVSSND LLTTIAWGVG KGITYALEGS
IFITGAAVQW FRDGLRAIDV SDEIEPLAGS VPDNGGVYFV PAFTGLGAPY WDPYARGLII
GITRGTTKAH IARAILESMA YQTMDVLGIM QRDSGIKIDA LKVDGGASKN DLLMQFQADI
LKMKVVRPKI METTSMGVAM LAGLSVGYWN SMDELKQKWK IDQVFEPKMD DEYREKLYSG
WKEAVRRALG WAKTIGG
