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Reviewed, UniProtKB/Swiss-Prot O42153 (G6PC_HAPNU)

Last modified November 4, 2008. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose-6-phosphatase
      Short name=G-6-Pase
      Short name=G6Pase
    EC=3.1.3.9
Gene names
Name: g6pc
Synonyms: g6pt
OrganismHaplochromis nubilus
Taxonomic identifier51172 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaPerciformesLabroideiCichlidaeAfrican cichlidsPseudocrenilabrinaeHaplochrominiHaplochromis

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the glucose-6-phosphatase family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucose-6-phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Glucose-6-phosphatase
PRO_0000087411

Regions

Topological domain1 – 2727Lumenal Potential
Transmembrane28 – 4821 Potential
Topological domain49 – 568Cytoplasmic Potential
Transmembrane57 – 7721 Potential
Topological domain78 – 11336Lumenal Potential
Transmembrane114 – 13421 Potential
Topological domain135 – 1417Cytoplasmic Potential
Transmembrane142 – 16221 Potential
Topological domain163 – 1664Lumenal Potential
Transmembrane167 – 18721 Potential
Topological domain188 – 20518Cytoplasmic Potential
Transmembrane206 – 22621 Potential
Topological domain227 – 25630Lumenal Potential
Transmembrane257 – 27620 Potential
Topological domain277 – 28913Cytoplasmic Potential
Transmembrane290 – 31021 Potential
Topological domain311 – 32414Lumenal Potential
Transmembrane325 – 34521 Potential
Topological domain346 – 3527Cytoplasmic Potential
Motif349 – 3524Prevents secretion from ER Potential

Sites

Active site1151Proton donor Potential
Active site1721Nucleophile By similarity
Binding site791Substrate Potential
Binding site1661Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
O42153-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7E9F1DF417298BAA

FASTA35239,904
        10         20         30         40         50         60 
MDLLHSWGVE LAVYLQTRYG KYEGLFDLAS TVADLHTTFF WLFPIWFHLR RDTALRLIWV 

        70         80         90        100        110        120 
AVIGDWLNLV LKWVLFGERP YWWVHETKFY GAGPAPSLQQ FPITCETGPG SPSGHAMGAA 

       130        140        150        160        170        180 
GVWYVMVTAL LSIAREKQCP PLLYRFLYIG LWMLMGLVEL VVCISRVYMA AHFPHQVIAG 

       190        200        210        220        230        240 
IITGTLVAEV VSKEKWIYSA SLKKYFLITL FLTSFAVGFY VLLKALDVDL LWTMEKAQKW 

       250        260        270        280        290        300 
CIRPEWVHLD SAPFASLLRN MGSLFGLGLG LHSPFYKTTK MRIMSAPLRI GCIVISVSLL 

       310        320        330        340        350 
HLLDGWTFSP ENHMTFYALS FGKSAVALLI PTTLVPWALS KIYPVKTEGK NL 

« Hide

References

[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: 10565541] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF008945 mRNA. Translation: AAB69285.1.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENO42153.

Family and domain databases

InterProIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PC_HAPNU
AccessionPrimary (citable) accession number: O42153
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 4, 2008
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents