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Database: UniProt
Entry: H6LBV3_ACEWD
LinkDB: H6LBV3_ACEWD
Original site: H6LBV3_ACEWD 
ID   H6LBV3_ACEWD            Unreviewed;       495 AA.
AC   H6LBV3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   Synonyms=glpK1 {ECO:0000313|EMBL:AFA47696.1};
GN   OrderedLocusNames=Awo_c09050 {ECO:0000313|EMBL:AFA47696.1};
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS   / WB1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA47696.1, ECO:0000313|Proteomes:UP000007177};
RN   [1] {ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RA   Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA   Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT   "Complete genome sequence of Acetobacterium woodii.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFA47696.1, ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RX   PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA   Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA   Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA   Gottschalk G., Muller V.;
RT   "An ancient pathway combining carbon dioxide fixation with the generation
RT   and utilization of a sodium ion gradient for ATP synthesis.";
RL   PLoS ONE 7:E33439-E33439(2012).
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   -!- 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00186}.
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DR   EMBL; CP002987; AFA47696.1; -; Genomic_DNA.
DR   RefSeq; WP_014355299.1; NC_016894.1.
DR   AlphaFoldDB; H6LBV3; -.
DR   STRING; 931626.Awo_c09050; -.
DR   KEGG; awo:Awo_c09050; -.
DR   eggNOG; COG0554; Bacteria.
DR   HOGENOM; CLU_009281_2_3_9; -.
DR   OMA; GQACYDV; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000007177; Chromosome.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007177};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00186}.
FT   DOMAIN          3..249
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          259..447
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   BINDING         11..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         242..243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         307
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         408..412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   495 AA;  54921 MW;  87D7E3451AFB6DE1 CRC64;
     MKYILGIDEG TTGVKVMIFD KSVNIIAQAY SEFTQHFPQS GWVEHDANEI WEVSLKMVAE
     ALKNGHIKPE EIEAIGITNQ RETTVFWDKK TGQPVCRAIV WQDRRTLDIC EALEAKDGAG
     IVDRTGMIIV PNDAATKIRW LLDNDPKVKK GVDEGELLYG TIDTWLVWKL TGGRVHVTDY
     SNASVTLLQN ARTLAYDDQI LNELQIPREI LPELRTSSEV YGMTDPTVFF GAEVAIAGIL
     GDQQAAAFGQ GCLEKGMAKN TYGTGSFMVM NTGSKYVPPS DGIFSPVLWS AKGRTDYGLE
     GMADVSGAVI QWLRDGLQMI NDTKEAEELA LQVKDSLGVY FVPAFVGLGA PYYDSYARGT
     IVGISRGTTK HHIARAALES MAFQVKDAFH VMEKKSGFKL TKLRADGGGA KSDFLLQFQA
     DILGIPVERP LITETTTLGA VYAAGLAVGY WDSFEEINEF WKIEKRFEPQ INEEKRQELC
     KFWNQAVERS AGWLK
//
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