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Q07982

- GFO_ZYMMO

UniProt

Q07982 - GFO_ZYMMO

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
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      Previous versions | rss
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    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

    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-SubCell

    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

    MTNKISSSDN LSNAVSATDD NASRTPNLTR RALVGGGVGL AAAGALASGL    50
    QAATLPAGAS QVPTTPAGRP MPYAIRPMPE DRRFGYAIVG LGKYALNQIL 100
    PGFAGCQHSR IEALVSGNAE KAKIVAAEYG VDPRKIYDYS NFDKIAKDPK 150
    IDAVYIILPN SLHAEFAIRA FKAGKHVMCE KPMATSVADC QRMIDAAKAA 200
    NKKLMIGYRC HYDPMNRAAV KLIRENQLGK LGMVTTDNSD VMDQNDPAQQ 250
    WRLRRELAGG GSLMDIGIYG LNGTRYLLGE EPIEVRAYTY SDPNDERFVE 300
    VEDRIIWQMR FRSGALSHGA SSYSTTTTSR FSVQGDKAVL LMDPATGYYQ 350
    NLISVQTPGH ANQSMMPQFI MPANNQFSAQ LDHLAEAVIN NKPVRSPGEE 400
    GMQDVRLIQA IYEAARTGRP VNTDWGYVRQ GGY 433
    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

    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 1, 2014
    This is version 107 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