ID A0A1A6GM61_NEOLE Unreviewed; 357 AA.
AC A0A1A6GM61;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glucose-6-phosphatase {ECO:0000256|PIRNR:PIRNR000905};
DE EC=3.1.3.9 {ECO:0000256|PIRNR:PIRNR000905};
GN ORFNames=A6R68_04538 {ECO:0000313|EMBL:OBS66949.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS66949.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS66949.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS66949.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS66949.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic
CC reticulum. Forms with the glucose-6-phosphate transporter
CC (SLC37A4/G6PT) the complex responsible for glucose production in the
CC terminal step of glycogenolysis and gluconeogenesis. Hence, it is the
CC key enzyme in homeostatic regulation of blood glucose levels.
CC {ECO:0000256|ARBA:ARBA00037155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + H2O = D-glucose + phosphate;
CC Xref=Rhea:RHEA:16689, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; EC=3.1.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000651};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000905}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009266, ECO:0000256|PIRNR:PIRNR000905}.
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:OBS66949.1}.
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DR EMBL; LZPO01087168; OBS66949.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6GM61; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd03381; PAP2_glucose_6_phosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR016275; Glucose-6-phosphatase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR12591; GLUCOSE-6-PHOSPHATASE; 1.
DR PANTHER; PTHR12591:SF3; GLUCOSE-6-PHOSPHATASE CATALYTIC SUBUNIT 1; 1.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000905};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|PIRNR:PIRNR000905};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000905};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000905};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..196
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
SQ SEQUENCE 357 AA; 40474 MW; EA8CD8355811E45A CRC64;
MEEGMNILHD FGIQSTHYLQ VNYEDSQDWF ILVSVIADLR NAFYVFFPIW FHIQETVGIN
LLWVAVVGDW INLVFKWILF GQRPYWWVLD TDYYSNTSVP LIKQFPVTCE TGPGSPSGHA
MGAAGVYYVM VTSTLAILRG KKKPTYGFRC LNIILWLGYW AVQLXVCLSR IYLAAHFPHQ
VVAGVLSGIA VAKTFSYIRG IYNASLKKYC LITFFLFGFA LGFYVLLKGL GVDLLWTLEK
AKRWCERPEW VHLDTTPFAS LFKNLGTLFG LGLALNSSMY RESCKGELRK LLPFRLACIV
TSLVLLHLFD NLKPPSQSEL IFYILSFCKS ATVPFAAVSL IPCCLARVLG QAHKKSL
//
