Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07982

- GFO_ZYMMO

UniProt

Q07982 - GFO_ZYMMO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucose--fructose oxidoreductase

Gene

gfo

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

Functioni

Catalytic activityi

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

Cofactori

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

Pathwayi

GO - Molecular functioni

  1. glucose-fructose oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. sorbitol biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13277.
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
ProteomesiUP000001173: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5252Tat-type signal1 PublicationPROSITE-ProRule annotationAdd
BLAST
Chaini53 – 433381Glucose--fructose oxidoreductasePRO_0000010851Add
BLAST

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.

Protein-protein interaction databases

STRINGi264203.ZMO0689.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 604
Beta strandi64 – 663
Beta strandi84 – 896
Helixi93 – 975
Helixi99 – 1024
Turni103 – 1053
Beta strandi107 – 1159
Helixi119 – 12810
Helixi133 – 1353
Beta strandi139 – 1413
Helixi142 – 1476
Beta strandi153 – 1564
Helixi160 – 1623
Helixi163 – 17210
Beta strandi176 – 1794
Beta strandi181 – 1833
Helixi187 – 20014
Beta strandi204 – 2063
Helixi209 – 2124
Helixi214 – 22411
Turni225 – 2284
Beta strandi230 – 23910
Helixi247 – 2504
Helixi251 – 2533
Helixi255 – 2584
Beta strandi259 – 2613
Helixi262 – 2654
Helixi267 – 27812
Beta strandi282 – 2909
Helixi296 – 2983
Beta strandi299 – 3013
Beta strandi303 – 3119
Beta strandi316 – 32510
Beta strandi328 – 33710
Beta strandi339 – 3468
Beta strandi353 – 3575
Beta strandi360 – 3645
Helixi376 – 38914
Beta strandi395 – 3973
Helixi398 – 41720

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 51-433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07982.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0673.
HOGENOMiHOG000227442.
KOiK00118.
OMAiHEFLTEP.
OrthoDBiEOG6RC3NJ.

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291T → N(PubMed:1537789)Curated
Sequence conflicti29 – 291T → N(PubMed:8472911)Curated
Sequence conflicti43 – 431A → R(PubMed:1537789)Curated
Sequence conflicti43 – 431A → R(PubMed:8472911)Curated
Sequence conflicti61 – 611Q → L in AAA27690. (PubMed:1537789)Curated
Sequence conflicti61 – 611Q → L in CAA51534. (PubMed:8472911)Curated
Sequence conflicti111 – 1199IEALVSGNA → MKLWSAVT in AAA27690. (PubMed:1537789)Curated
Sequence conflicti170 – 1701A → S in AAA27690. (PubMed:1537789)Curated
Sequence conflicti247 – 25812PAQQW…RRELA → LHSSGVCVVNS in AAA27690. (PubMed:1537789)CuratedAdd
BLAST
Sequence conflicti420 – 4201P → A in AAA27690. (PubMed:1537789)Curated
Sequence conflicti431 – 4333GGY → VVIDSDLTYLG in AAA27690. (PubMed:1537789)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_162424.1. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV89313; AAV89313; ZMO0689.
GeneIDi3187982.
KEGGizmo:ZMO0689.
PATRICi32566692. VBIZymMob102260_0654.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A42289.
RefSeqi WP_011240581.1. NC_006526.2.
YP_162424.1. NC_006526.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q07982.
SMRi Q07982. Positions 51-433.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264203.ZMO0689.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV89313 ; AAV89313 ; ZMO0689 .
GeneIDi 3187982.
KEGGi zmo:ZMO0689.
PATRICi 32566692. VBIZymMob102260_0654.

Phylogenomic databases

eggNOGi COG0673.
HOGENOMi HOG000227442.
KOi K00118.
OMAi HEFLTEP.
OrthoDBi EOG6RC3NJ.

Enzyme and pathway databases

UniPathwayi UPA00815 ; UER00784 .
BioCyci MetaCyc:MONOMER-13277.

Miscellaneous databases

EvolutionaryTracei Q07982.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR008354. Glc-Fru_OxRdtase_bac.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view ]
PRINTSi PR01775. GLFROXRDTASE.
PROSITEi PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

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: October 29, 2014
This is version 108 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

External Data

Dasty 3