ID   G6PC1_HAPXE             Reviewed;         277 AA.
AC   O42154;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Glucose-6-phosphatase catalytic subunit 1;
DE            EC=3.1.3.9 {ECO:0000250|UniProtKB:P35575};
DE   AltName: Full=Glucose-6-phosphatase;
DE            Short=G-6-Pase;
DE            Short=G6Pase;
DE   Flags: Fragment;
GN   Name=g6pc1; Synonyms=g6pc, g6pt;
OS   Haplochromis xenognathus (Lake Victoria cichlid) (Ptyochromis xenognathus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=51185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10565541; DOI=10.3109/10425179909033932;
RA   Nagl S., Mayer W.E., Klein J.;
RT   "Isolation and sequencing of cDNA clones coding for the catalytic unit of
RT   glucose-6-phosphatase from two haplochromine cichlid fishes.";
RL   DNA Seq. 10:25-29(1999).
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:0000250|UniProtKB:P35575}.
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:0000250|UniProtKB:P35575};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000250|UniProtKB:P35575}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P35575}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
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DR   EMBL; AF008946; AAB69286.1; -; mRNA.
DR   AlphaFoldDB; O42154; -.
DR   SMR; O42154; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004346; F:glucose-6-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Gluconeogenesis; Hydrolase; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..277
FT                   /note="Glucose-6-phosphatase catalytic subunit 1"
FT                   /id="PRO_0000087412"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           274..277
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         4
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   277 AA;  30971 MW;  9A05E82DFE1DA4A0 CRC64;
     FGERPYWWVH ETKFYGAGPA PSLQQFPITC ETGPGSPSGH AMGAAGVWYV MVTALLSIAR
     EKQCPPLLYR FLYIGLWMLM GLVELVVCIS RVYMAAHFPH QVIAGIITGT LVAEVVSKEK
     WIYSASLKKY FLITLFLTSF AVGFYVLLKA LDVDLLWTME KAQKWCIRPE WVHLDSAPFA
     SLLRNMGSLF GLGLGLHSPF YKTTKMRIMS APLRIGCIVI SVSLLHLLDG WTFSPENHMT
     FYALSFGKSA VALLIPTTLV PWALSKIYPV KTEGKNL