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Protein

Glucose--fructose oxidoreductase

Gene

gfo

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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

Pathwayi: D-sorbitol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-sorbitol from D-fructose and D-glucose.
Proteins known to be involved in this subpathway in this organism are:
  1. Glucose--fructose oxidoreductase (gfo)
This subpathway is part of the pathway D-sorbitol biosynthesis, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-sorbitol from D-fructose and D-glucose, the pathway D-sorbitol biosynthesis and in Carbohydrate metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13277.
BRENDAi1.1.99.28. 6765.
UniPathwayiUPA00815; UER00784.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose--fructose oxidoreductase (EC:1.1.99.28)
Short name:
GFOR
Gene namesi
Name:gfo
Ordered Locus Names:ZMO0689
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 52Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST52
ChainiPRO_000001085153 – 433Glucose--fructose oxidoreductaseAdd BLAST381

Post-translational modificationi

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

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi57 – 60Combined sources4
Beta strandi64 – 66Combined sources3
Beta strandi84 – 89Combined sources6
Helixi93 – 97Combined sources5
Helixi99 – 102Combined sources4
Turni103 – 105Combined sources3
Beta strandi107 – 115Combined sources9
Helixi119 – 128Combined sources10
Helixi133 – 135Combined sources3
Beta strandi139 – 141Combined sources3
Helixi142 – 147Combined sources6
Beta strandi153 – 156Combined sources4
Helixi160 – 162Combined sources3
Helixi163 – 172Combined sources10
Beta strandi176 – 179Combined sources4
Beta strandi181 – 183Combined sources3
Helixi187 – 200Combined sources14
Beta strandi204 – 206Combined sources3
Helixi209 – 212Combined sources4
Helixi214 – 224Combined sources11
Turni225 – 228Combined sources4
Beta strandi230 – 239Combined sources10
Helixi247 – 250Combined sources4
Helixi251 – 253Combined sources3
Helixi255 – 258Combined sources4
Beta strandi259 – 261Combined sources3
Helixi262 – 265Combined sources4
Helixi267 – 278Combined sources12
Beta strandi282 – 290Combined sources9
Helixi296 – 298Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi303 – 311Combined sources9
Beta strandi316 – 325Combined sources10
Beta strandi328 – 337Combined sources10
Beta strandi339 – 346Combined sources8
Beta strandi353 – 357Combined sources5
Beta strandi360 – 364Combined sources5
Helixi376 – 389Combined sources14
Beta strandi395 – 397Combined sources3
Helixi398 – 417Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ07982.
SMRiQ07982.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07982.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000227442.
KOiK00118.
OMAiHEFLTEP.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR008354. Glc-Fru_OxRdtase_bac.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
PRINTSiPR01775. GLFROXRDTASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07982-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNKISSSDN LSNAVSATDD NASRTPNLTR RALVGGGVGL AAAGALASGL
60 70 80 90 100
QAATLPAGAS QVPTTPAGRP MPYAIRPMPE DRRFGYAIVG LGKYALNQIL
110 120 130 140 150
PGFAGCQHSR IEALVSGNAE KAKIVAAEYG VDPRKIYDYS NFDKIAKDPK
160 170 180 190 200
IDAVYIILPN SLHAEFAIRA FKAGKHVMCE KPMATSVADC QRMIDAAKAA
210 220 230 240 250
NKKLMIGYRC HYDPMNRAAV KLIRENQLGK LGMVTTDNSD VMDQNDPAQQ
260 270 280 290 300
WRLRRELAGG GSLMDIGIYG LNGTRYLLGE EPIEVRAYTY SDPNDERFVE
310 320 330 340 350
VEDRIIWQMR FRSGALSHGA SSYSTTTTSR FSVQGDKAVL LMDPATGYYQ
360 370 380 390 400
NLISVQTPGH ANQSMMPQFI MPANNQFSAQ LDHLAEAVIN NKPVRSPGEE
410 420 430
GMQDVRLIQA IYEAARTGRP VNTDWGYVRQ GGY
Length:433
Mass (Da):47,190
Last modified:February 15, 2005 - v2
Checksum:i13CFADE84794E736
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29T → N (PubMed:1537789).Curated1
Sequence conflicti29T → N (PubMed:8472911).Curated1
Sequence conflicti43A → R (PubMed:1537789).Curated1
Sequence conflicti43A → R (PubMed:8472911).Curated1
Sequence conflicti61Q → L in AAA27690 (PubMed:1537789).Curated1
Sequence conflicti61Q → L in CAA51534 (PubMed:8472911).Curated1
Sequence conflicti111 – 119IEALVSGNA → MKLWSAVT in AAA27690 (PubMed:1537789).Curated9
Sequence conflicti170A → S in AAA27690 (PubMed:1537789).Curated1
Sequence conflicti247 – 258PAQQW…RRELA → LHSSGVCVVNS in AAA27690 (PubMed:1537789).CuratedAdd BLAST12
Sequence conflicti420P → A in AAA27690 (PubMed:1537789).Curated1
Sequence conflicti431 – 433GGY → VVIDSDLTYLG in AAA27690 (PubMed:1537789).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97379 Genomic DNA. Translation: AAA27690.1.
Z80356 Genomic DNA. Translation: CAB02496.1.
AE008692 Genomic DNA. Translation: AAV89313.1.
X73088 Genomic DNA. Translation: CAA51534.1.
PIRiA42289.
RefSeqiWP_011240581.1. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV89313; AAV89313; ZMO0689.
KEGGiag:AAA27690.
zmo:ZMO0689.
PATRICi32566692. VBIZymMob102260_0654.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97379 Genomic DNA. Translation: AAA27690.1.
Z80356 Genomic DNA. Translation: CAB02496.1.
AE008692 Genomic DNA. Translation: AAV89313.1.
X73088 Genomic DNA. Translation: CAA51534.1.
PIRiA42289.
RefSeqiWP_011240581.1. NC_006526.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ07982.
SMRiQ07982.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV89313; AAV89313; ZMO0689.
KEGGiag:AAA27690.
zmo:ZMO0689.
PATRICi32566692. VBIZymMob102260_0654.

Phylogenomic databases

HOGENOMiHOG000227442.
KOiK00118.
OMAiHEFLTEP.

Enzyme and pathway databases

UniPathwayiUPA00815; UER00784.
BioCyciMetaCyc:MONOMER-13277.
BRENDAi1.1.99.28. 6765.

Miscellaneous databases

EvolutionaryTraceiQ07982.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR008354. Glc-Fru_OxRdtase_bac.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
PRINTSiPR01775. GLFROXRDTASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGFO_ZYMMO
AccessioniPrimary (citable) accession number: Q07982
Secondary accession number(s): P75002, Q5NPP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.