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Q7NVH4 (G6PI2_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase 2

Short name=GPI 2
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase 2
Short name=PGI 2
Phosphohexose isomerase 2
Short name=PHI 2
Gene names
Name:pgi2
Ordered Locus Names:CV_2369
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00473.

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: UniProtKB-HAMAP

glycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Glucose-6-phosphate isomerase 2 HAMAP-Rule MF_00473
PRO_0000180625

Sites

Active site3571Proton donor By similarity
Active site3881 By similarity
Active site5141 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NVH4 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: EF08BD1CE44301AD

FASTA55061,928
        10         20         30         40         50         60 
MAAQRHIDIN STQVWAKLHQ HQRATRHMHM RELFELDPQR FQRFSLELDG LLLDYSKNRV 

        70         80         90        100        110        120 
TERTLELLFD LARKADLRGW MDRMRSGERI NVSENRSVLH TALRLPAGAR LDLEGHNVAA 

       130        140        150        160        170        180 
DVHQVLARLK DFSEQVREGR WLGFAGQPIR DVVNLGIGGS DLGPLVAADA LAAYAHPDLK 

       190        200        210        220        230        240 
VHFVSNVDGQ HLARTLERLN PATTLFIVAS KSFTTPETLL NAQAARAWFL QAAGEAQIAK 

       250        260        270        280        290        300 
HFVAVSTNEP AVRAFGIDPQ HMFGFWDWVG GRYSVWSAIG LPVMLSIGYD NFRAFLDGGH 

       310        320        330        340        350        360 
AMDRHFFESP FDANMPVLLA LIGIWYNTFY RAHTHAIMPY DHGLRRLPAH IQQLDMESNG 

       370        380        390        400        410        420 
KRVGRLGEAL DFDTGPVIWG EEGANSQHAF FQLLHQGTRL VPCDFILPLN SHYPLGNQHD 

       430        440        450        460        470        480 
VLVANCLAQT EALMRGKNEA EVMRELSHLS GEQLDMLLPQ KLFPGNQPSN TLALDRVTPY 

       490        500        510        520        530        540 
SMGMLMALYE HKVFVQGVIW GINSFDQWGV EYGKQLARRI LPELSGDTGA LGHDSSTNGL 

       550 
IRHYRERHGK 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ60041.1.
RefSeqNP_902039.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NVH4.
SMRQ7NVH4. Positions 8-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_2369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ60041; AAQ60041; CV_2369.
GeneID2546984.
KEGGcvi:CV_2369.
PATRIC21439504. VBIChrVio67196_2307.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMACELAREC.
OrthoDBEOG64R61J.
ProtClustDBCLSK2485482.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-2425-MONOMER.
UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 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 nameG6PI2_CHRVO
AccessionPrimary (citable) accession number: Q7NVH4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways