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Reviewed, UniProtKB/Swiss-Prot Q7P1R4 (G6PI1_CHRVO)

Last modified November 3, 2009. Version 42. 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-phosphate isomerase 1
      Short name=GPI 1
    EC=5.3.1.9
Alternative name(s):
    Phosphoglucose isomerase 1
      Short name=PGI 1
    Phosphohexose isomerase 1
      Short name=PHI 1
Gene names
Name: pgi1
Ordered Locus Names: CV_0149
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP MF_00473

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP MF_00473

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: HAMAP

glycolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 547547Glucose-6-phosphate isomerase 1 HAMAP MF_00473
PRO_0000180624

Sites

Active site3531Proton donor By similarity
Active site3841 By similarity
Active site5121 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7P1R4-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: F264B1BFD1E23DB7

FASTA54761,073
        10         20         30         40         50         60 
MSELTELPAW QALWDHFAEA KHLHMRDLFA ADPGRAERYS LEVGGLFLDY SKNRITDATL 

        70         80         90        100        110        120 
LGLMELAREA GLPARIKAMF KGEKINRTEN RAVLHVALRN RTNSPIRVDG EDVMPKVNSV 

       130        140        150        160        170        180 
LERMGKFAHA VRSGDWLGFT NQPITDIVNI GIGGSDLGPL MVCSALKPFG HPRLNMHFVS 

       190        200        210        220        230        240 
NVDGAQLKET LKKVHPETTL FVVESKTFTT QETLTNALTA REWFLSHARD EGAVAKHFVA 

       250        260        270        280        290        300 
VSTNQKAVAE FGIDPANMFE FWNWVGGRYS LWSAIGLPIM LYLGEENFTE LLNGAHIMDQ 

       310        320        330        340        350        360 
HFMNAPFEQN MPVLLAMIGV WYINYYGGGS HVIAPYDQYL HRLPAFIQQL DMESNGKQVT 

       370        380        390        400        410        420 
LSGQPVDFET APIIWGETGI NGQHAFFQLL HQGTHISPID LIASLGNRAS LPGHHEILLA 

       430        440        450        460        470        480 
NVFAQAEAFM RGKTADEVRA ELAEQGLSGE EMEALVPHKV FGGNRPTNTL LMSRLDPRNL 

       490        500        510        520        530        540 
GSLIALYEHK IFVQGVIWHI NSFDQWGVEL GKQLAKTIHA ELTGKLEQAE HDSSTRRLIQ 


LYRKANG 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ57828.1.
RefSeqNP_899819.1.

3D structure databases

HSSPHSSP built from PDB template 1JIQ based on UniProtKB P06744.
ModBaseSearch...

Genome annotation databases

GeneID2550708.
GenomeReviewsGene locus CV_0149 in contig AE016825_GR.
KEGGcvi:CV_0149.
NMPDRfig|243365.1.peg.149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7P1R4.
OMAGPKIVSQ.

Enzyme and pathway databases

BioCycCVIO243365:CV_0149-MON.
BRENDA5.3.1.9. 415.

Family and domain databases

HAMAPMF_00473.
[Tree]
InterProIPR001672. G6P_Isomerase.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. G6P_Isomerase. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PI1_CHRVO
AccessionPrimary (citable) accession number: Q7P1R4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 15, 2003
Last modified: November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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