Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucose-6-phosphatase

Gene

g6pc

Organism
Haplochromis nubilus (Blue Victoria mouthbrooder) (Tilapia nubila)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

D-glucose 6-phosphate + H2O = D-glucose + phosphate.

Pathway:igluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791SubstrateSequence Analysis
Active sitei115 – 1151Proton donorSequence Analysis
Binding sitei166 – 1661SubstrateSequence Analysis
Active sitei172 – 1721NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Gluconeogenesis

Enzyme and pathway databases

UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphatase (EC:3.1.3.9)
Short name:
G-6-Pase
Short name:
G6Pase
Gene namesi
Name:g6pc
Synonyms:g6pt
OrganismiHaplochromis nubilus (Blue Victoria mouthbrooder) (Tilapia nubila)
Taxonomic identifieri51172 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataOvalentariaCichlomorphaeCichliformesCichlidaeAfrican cichlidsPseudocrenilabrinaeHaplochrominiHaplochromis

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2727LumenalSequence AnalysisAdd
BLAST
Transmembranei28 – 4821HelicalSequence AnalysisAdd
BLAST
Topological domaini49 – 568CytoplasmicSequence Analysis
Transmembranei57 – 7721HelicalSequence AnalysisAdd
BLAST
Topological domaini78 – 11336LumenalSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Topological domaini135 – 1417CytoplasmicSequence Analysis
Transmembranei142 – 16221HelicalSequence AnalysisAdd
BLAST
Topological domaini163 – 1664LumenalSequence Analysis
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST
Topological domaini188 – 20518CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence AnalysisAdd
BLAST
Topological domaini227 – 25630LumenalSequence AnalysisAdd
BLAST
Transmembranei257 – 27620HelicalSequence AnalysisAdd
BLAST
Topological domaini277 – 28913CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST
Topological domaini311 – 32414LumenalSequence AnalysisAdd
BLAST
Transmembranei325 – 34521HelicalSequence AnalysisAdd
BLAST
Topological domaini346 – 3527CytoplasmicSequence Analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Glucose-6-phosphatasePRO_0000087411Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO42153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi349 – 3524Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the glucose-6-phosphatase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003560.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFiPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

O42153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLLHSWGVE LAVYLQTRYG KYEGLFDLAS TVADLHTTFF WLFPIWFHLR
60 70 80 90 100
RDTALRLIWV AVIGDWLNLV LKWVLFGERP YWWVHETKFY GAGPAPSLQQ
110 120 130 140 150
FPITCETGPG SPSGHAMGAA GVWYVMVTAL LSIAREKQCP PLLYRFLYIG
160 170 180 190 200
LWMLMGLVEL VVCISRVYMA AHFPHQVIAG IITGTLVAEV VSKEKWIYSA
210 220 230 240 250
SLKKYFLITL FLTSFAVGFY VLLKALDVDL LWTMEKAQKW CIRPEWVHLD
260 270 280 290 300
SAPFASLLRN MGSLFGLGLG LHSPFYKTTK MRIMSAPLRI GCIVISVSLL
310 320 330 340 350
HLLDGWTFSP ENHMTFYALS FGKSAVALLI PTTLVPWALS KIYPVKTEGK

NL
Length:352
Mass (Da):39,904
Last modified:January 1, 1998 - v1
Checksum:i7E9F1DF417298BAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008945 mRNA. Translation: AAB69285.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008945 mRNA. Translation: AAB69285.1.

3D structure databases

ProteinModelPortaliO42153.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003560.

Enzyme and pathway databases

UniPathwayiUPA00138.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFiPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and sequencing of cDNA clones coding for the catalytic unit of glucose-6-phosphatase from two haplochromine cichlid fishes."
    Nagl S., Mayer W.E., Klein J.
    DNA Seq. 10:25-29(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiG6PC_HAPNU
AccessioniPrimary (citable) accession number: O42153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.