ID G6PC1_HAPNU Reviewed; 352 AA. AC O42153; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 22-FEB-2023, entry version 75. 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; GN Name=g6pc1; Synonyms=g6pc, g6pt; OS Haplochromis nubilus (Blue Victoria mouthbrooder) (Tilapia nubila). 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=51172; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF008945; AAB69285.1; -; mRNA. DR AlphaFoldDB; O42153; -. DR UniPathway; UPA00138; -. 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-UniPathway. 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:SF5; GLUCOSE-6-PHOSPHATASE; 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 2: Evidence at transcript level; KW Endoplasmic reticulum; Gluconeogenesis; Hydrolase; Membrane; Transmembrane; KW Transmembrane helix. FT CHAIN 1..352 FT /note="Glucose-6-phosphatase catalytic subunit 1" FT /id="PRO_0000087411" FT TOPO_DOM 1..27 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 28..48 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 49..56 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 57..77 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 78..113 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 135..141 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 142..162 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 163..166 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 167..187 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 188..205 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 227..256 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 257..276 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 277..289 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 311..324 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P35575" FT TRANSMEM 325..345 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 346..352 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P35575" FT MOTIF 349..352 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255" FT ACT_SITE 115 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 172 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P35575" FT BINDING 79 FT /ligand="substrate" FT /evidence="ECO:0000255" FT BINDING 166 FT /ligand="substrate" FT /evidence="ECO:0000255" SQ SEQUENCE 352 AA; 39904 MW; 7E9F1DF417298BAA CRC64; MDLLHSWGVE LAVYLQTRYG KYEGLFDLAS TVADLHTTFF WLFPIWFHLR RDTALRLIWV AVIGDWLNLV LKWVLFGERP YWWVHETKFY GAGPAPSLQQ FPITCETGPG SPSGHAMGAA GVWYVMVTAL LSIAREKQCP PLLYRFLYIG LWMLMGLVEL VVCISRVYMA AHFPHQVIAG IITGTLVAEV VSKEKWIYSA SLKKYFLITL FLTSFAVGFY VLLKALDVDL LWTMEKAQKW CIRPEWVHLD SAPFASLLRN MGSLFGLGLG LHSPFYKTTK MRIMSAPLRI GCIVISVSLL HLLDGWTFSP ENHMTFYALS FGKSAVALLI PTTLVPWALS KIYPVKTEGK NL //