Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q07982 (GFO_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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--fructose oxidoreductase

Short name=GFOR
EC=1.1.99.28
Gene names
Name:gfo
Ordered Locus Names:ZMO0689
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glucose + D-fructose = D-gluconolactone + D-glucitol.

Cofactor

Binds 1 NADP+ per subunit. The NADP cannot dissociate.

Pathway

Carbohydrate metabolism; D-sorbitol biosynthesis; D-sorbitol from D-fructose and D-glucose: step 1/1.

Subunit structure

Homotetramer.

Subcellular location

Periplasm.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the Gfo/Idh/MocA family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processsorbitol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-fructose oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5252Tat-type signal Ref.1
Chain53 – 433381Glucose--fructose oxidoreductase
PRO_0000010851

Experimental info

Sequence conflict291T → N Ref.1
Sequence conflict291T → N Ref.4
Sequence conflict431A → R Ref.1
Sequence conflict431A → R Ref.4
Sequence conflict611Q → L in AAA27690. Ref.1
Sequence conflict611Q → L in CAA51534. Ref.4
Sequence conflict111 – 1199IEALVSGNA → MKLWSAVT in AAA27690. Ref.1
Sequence conflict1701A → S in AAA27690. Ref.1
Sequence conflict247 – 25812PAQQW…RRELA → LHSSGVCVVNS in AAA27690. Ref.1
Sequence conflict4201P → A in AAA27690. Ref.1
Sequence conflict431 – 4333GGY → VVIDSDLTYLG in AAA27690. Ref.1

Secondary structure

........................................................................ 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07982 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: 13CFADE84794E736

FASTA43347,190
        10         20         30         40         50         60 
MTNKISSSDN LSNAVSATDD NASRTPNLTR RALVGGGVGL AAAGALASGL QAATLPAGAS 

        70         80         90        100        110        120 
QVPTTPAGRP MPYAIRPMPE DRRFGYAIVG LGKYALNQIL PGFAGCQHSR IEALVSGNAE 

       130        140        150        160        170        180 
KAKIVAAEYG VDPRKIYDYS NFDKIAKDPK IDAVYIILPN SLHAEFAIRA FKAGKHVMCE 

       190        200        210        220        230        240 
KPMATSVADC QRMIDAAKAA NKKLMIGYRC HYDPMNRAAV KLIRENQLGK LGMVTTDNSD 

       250        260        270        280        290        300 
VMDQNDPAQQ WRLRRELAGG GSLMDIGIYG LNGTRYLLGE EPIEVRAYTY SDPNDERFVE 

       310        320        330        340        350        360 
VEDRIIWQMR FRSGALSHGA SSYSTTTTSR FSVQGDKAVL LMDPATGYYQ NLISVQTPGH 

       370        380        390        400        410        420 
ANQSMMPQFI MPANNQFSAQ LDHLAEAVIN NKPVRSPGEE GMQDVRLIQA IYEAARTGRP 

       430 
VNTDWGYVRQ GGY 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis."
Kanagasundaram V., Scopes R.K.
J. Bacteriol. 174:1439-1447(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-87.
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[2]"Export of the periplasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis."
Wiegert T., Sahm H., Sprenger G.A.
Arch. Microbiol. 166:32-41(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[3]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[4]"Glucose-fructose oxidoreductase, a periplasmic enzyme of Zymomonas mobilis, is active in its precursor form."
Loos H., Sahm H., Sprenger G.A.
FEMS Microbiol. Lett. 107:293-298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71, PROTEIN SEQUENCE OF 2-16 AND 53-71.
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6 and ATCC 31821 / ZM4 / CP4.
[5]"The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP."
Kingston R.L., Scopes R.K., Baker E.N.
Structure 4:1413-1428(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97379 Genomic DNA. Translation: AAA27690.1.
Z80356 Genomic DNA. Translation: CAB02496.1.
AE008692 Genomic DNA. Translation: AAV89313.1.
X73088 Genomic DNA. Translation: CAA51534.1.
PIRA42289.
RefSeqYP_162424.1. NC_006526.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVJX-ray2.70A/B/C/D82-433[»]
1H6AX-ray2.50A/B1-433[»]
1H6BX-ray2.60A/B1-433[»]
1H6CX-ray2.20A/B1-433[»]
1H6DX-ray2.05A/B/C/D/E/F/G/H/I/J/K/L1-433[»]
1OFGX-ray2.70A/B/C/D/E/F53-433[»]
1RYDX-ray2.20A/B53-433[»]
1RYEX-ray2.30A/B/C/D53-433[»]
ProteinModelPortalQ07982.
SMRQ07982. Positions 51-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO0689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89313; AAV89313; ZMO0689.
GeneID3187982.
KEGGzmo:ZMO0689.
PATRIC32566692. VBIZymMob102260_0654.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0673.
HOGENOMHOG000227442.
KOK00118.
OMAHEFLTEP.
OrthoDBEOG6RC3NJ.
ProtClustDBCLSK2524643.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13277.
UniPathwayUPA00815; UER00784.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR008354. Glc-Fru_OxRdtase_bac.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
IPR006311. TAT_signal.
[Graphical view]
PfamPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
PRINTSPR01775. GLFROXRDTASE.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ07982.

Entry information

Entry nameGFO_ZYMMO
AccessionPrimary (citable) accession number: Q07982
Secondary accession number(s): P75002, Q5NPP7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 15, 2005
Last modified: November 13, 2013
This is version 103 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways