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Protein

Glucose--fructose oxidoreductase

Gene

gfo

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionOxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13277
ZMOB264203:G1FZK-618-MONOMER
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

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB02379 Beta-D-Glucose
DB03345 Beta-Mercaptoethanol
DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 52Tat-type signalPROSITE-ProRule annotation2 PublicationsAdd 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.

Proteomic databases

PRIDEiQ07982

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
OMAiHNAYGPD

Family and domain databases

InterProiView protein in InterPro
IPR008354 Glc-Fru_OxRdtase_bac
IPR036291 NAD(P)-bd_dom_sf
IPR000683 Oxidoreductase_N
IPR004104 OxRdtase_C
IPR006311 TAT_signal
PfamiView protein in Pfam
PF01408 GFO_IDH_MocA, 1 hit
PF02894 GFO_IDH_MocA_C, 1 hit
PRINTSiPR01775 GLFROXRDTASE
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS51318 TAT, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiGFO_ZYMMO
AccessioniPrimary (citable) accession number: Q07982
Secondary accession number(s): P75002, Q5NPP7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 15, 2005
Last modified: May 23, 2018
This is version 127 of the entry and version 2 of the sequence. See 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

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