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Database: UniProt
Entry: F1Z2V5_9STRE
LinkDB: F1Z2V5_9STRE
Original site: F1Z2V5_9STRE 
ID   F1Z2V5_9STRE            Unreviewed;       503 AA.
AC   F1Z2V5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
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:EGE54563.1};
GN   ORFNames=SPB_1185 {ECO:0000313|EMBL:EGE54563.1};
OS   Streptococcus parauberis NCFD 2020.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE54563.1, ECO:0000313|Proteomes:UP000003732};
RN   [1] {ECO:0000313|EMBL:EGE54563.1, ECO:0000313|Proteomes:UP000003732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE54563.1,
RC   ECO:0000313|Proteomes:UP000003732};
RA   Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA   Town C.D.;
RL   Submitted (FEB-2011) 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: Activated by phosphorylation and inhibited by
CC       fructose 1,6-bisphosphate (FBP). {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   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium).
CC       {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system
CC       (PTS), including enzyme I, and histidine-containing protein (HPr) are
CC       required for the phosphorylation, which leads to the activation of the
CC       enzyme. {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: 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:EGE54563.1}.
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DR   EMBL; AEUT02000001; EGE54563.1; -; Genomic_DNA.
DR   RefSeq; WP_003105149.1; NZ_AEUT02000001.1.
DR   AlphaFoldDB; F1Z2V5; -.
DR   GeneID; 66816966; -.
DR   eggNOG; COG0554; Bacteria.
DR   HOGENOM; CLU_009281_2_3_9; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000003732; 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}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00186};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00186}.
FT   DOMAIN          6..253
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          263..451
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   BINDING         14..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         84..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         246..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         330
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         412..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   MOD_RES         232
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   503 AA;  55505 MW;  1D6DC60B4A6A05B3 CRC64;
     MTEEKYIMAI DQGTTSSRAI IFNKKGEKIA SSQKEFPQIF PQAGWVEHNA NQIWNSVQSV
     IAGAFIESSI KPGQIEAIGI TNQRETTVVW DKATGLPIYN AIVWQSRQTA PIADQLKQDG
     HIDLIHEKTG LVIDAYFSAT KIRWILDHVP GAQERAEKGE LLFGTIDTWL VWKLTDGAVH
     VTDYSNAART MLYNIKDLSW DDEILSILNI PKAMLPEVKS NSEIYGKTAP FHFYGGEIPI
     SGMAGDQQAA LFGQLAFEPG MVKNTYGTGS FIIMNTGEEM QLSENNLLTT IGYGINGKVY
     YALEGSIFIA GSAIQWLRDG LRMIETSPES EELAKLSKSD DEIYVVPAFT GLGAPYWDSN
     ARGSVFGLTR GTTKEDFVKA TLQSIAYQVR DVIDTMQDES GIDIPQLRVD GGAAMNDLLM
     QFQADILGID IARAKNLETT ALGAAFLAGL AVGYWEDLDS LKELNATGKL FKSSMNESRK
     EKLYKGWKKA VKATQLFATD EDE
//
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