Glucose--fructose oxidoreductase precursor - Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

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Q07982 (GFO_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glucose--fructose oxidoreductase
Short name=GFOR
EC=1.1.99.28

Gene names

Name:	gfo
Ordered Locus Names:	ZMO0689

Organism

Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]

Taxonomic identifier

264203 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas ›

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Periplasm
Domain	Signal
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	sorbitol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glucose-fructose oxidoreductase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 52

Tat-type signal Ref.1

Chain

53 – 433

381

Glucose--fructose oxidoreductase

PRO_0000010851

Experimental info

Sequence conflict

T → N Ref.1

Sequence conflict

T → N Ref.4

Sequence conflict

A → R Ref.1

Sequence conflict

A → R Ref.4

Sequence conflict

Q → L in AAA27690. Ref.1

Sequence conflict

Q → L in CAA51534. Ref.4

Sequence conflict

111 – 119

IEALVSGNA → MKLWSAVT in AAA27690. Ref.1

Sequence conflict

170

A → S in AAA27690. Ref.1

Sequence conflict

247 – 258

PAQQW…RRELA → LHSSGVCVVNS in AAA27690. Ref.1

Sequence conflict

420

P → A in AAA27690. Ref.1

Sequence conflict

431 – 433

GGY → VVIDSDLTYLG in AAA27690. Ref.1

Secondary structure

433

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q07982 [UniParc].

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

FASTA

433

47,190

        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' referencesShow '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. , 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.

PIR

A42289.

RefSeq

YP_162424.1. NC_006526.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EVJ	X-ray	2.70	A/B/C/D	82-433	[»]
1H6A	X-ray	2.50	A/B	1-433	[»]
1H6B	X-ray	2.60	A/B	1-433	[»]
1H6C	X-ray	2.20	A/B	1-433	[»]
1H6D	X-ray	2.05	A/B/C/D/E/F/G/H/I/J/K/L	1-433	[»]
1OFG	X-ray	2.70	A/B/C/D/E/F	53-433	[»]
1RYD	X-ray	2.20	A/B	53-433	[»]
1RYE	X-ray	2.30	A/B/C/D	53-433	[»]

ProteinModelPortal

Q07982.

SMR

Q07982. Positions 51-433.

ModBase

Search...

Protein-protein interaction databases

STRING

264203.ZMO0689.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV89313; AAV89313; ZMO0689.

GeneID

3187982.

KEGG

zmo:ZMO0689.

PATRIC

32566692. VBIZymMob102260_0654.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0673.

HOGENOM

HOG000227442.

K00118.

OMA

ANATHAE.

ProtClustDB

CLSK2524643.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13277.

UniPathway

UPA00815; UER00784.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR008354. Glc-Fru_OxRdtase_bac.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
IPR006311. TAT_signal.
[Graphical view]

Pfam

PF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]

PRINTS

PR01775. GLFROXRDTASE.

PROSITE

PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q07982.

Entry information

Entry name

GFO_ZYMMO

Accession

Primary (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:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents