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Protein

5-(hydroxymethyl)furfural oxidase

Gene

MPQ_0130

Organism
Methylovorus sp. (strain MP688)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation (PubMed:24271187, PubMed:24802551). To a lesser extent, is also able to catalyze the oxidation of thiols that are structurally similar to its alcohol substrates, yielding the corresponding thiocarbonyls (PubMed:25284255).3 Publications

Miscellaneous

At pH 7.0, phenylmethanethiol is oxidized to the corresponding aromatic thioaldehyde, benzothialdehyde, and no formation of 1,2-dibenzyldisulfane is observed, demonstrating that HMFO does not catalyze the formation of disulfide bonds. At pH 8.0, two products are formed, benzothialdehyde and benzaldehyde; this suggests that the thioaldehyde is slowly hydrated, yielding the aldehyde as the final product.1 Publication

Catalytic activityi

5-(hydroxymethyl)furfural + 3 O2 + 2 H2O = furan-2,5-dicarboxylate + 3 H2O2.2 Publications
Phenylmethanethiol + O2 = benzothialdehyde + H2O2.1 Publication

Cofactori

FAD1 Publication1 Publication

Kineticsi

kcat is 9.9 sec(-1) with 5-(hydroxymethyl)furfural as substrate. kcat is 21.1 sec(-1) with 1,4-benzenedimethanol as substrate. kcat is 14.0 sec(-1) with 1,3-benzenedimethanol as substrate. kcat is 13.5 sec(-1) with benzyl alcohol as substrate. kcat is 7.2 sec(-1) with 4-hydroxybenzyl alcohol as substrate. kcat is 17.1 sec(-1) with 4-aminobenzyl alcohol as substrate. kcat is 9.5 sec(-1) with 4-chlorobenzyl alcohol as substrate. kcat is 17.0 sec(-1) with cinnamyl alcohol as substrate. kcat is 13.3 sec(-1) with 2,4-hexadien-1-ol as substrate. kcat is 21.0 sec(-1) with vanillyl alcohol as substrate (PubMed:24271187). kcat is 2.1 sec(-1) with phenylmethanethiol as substrate. kcat is 3.0 sec(-1) with (4-nitrophenyl)phenylmethanethiol as substrate. kcat is 4.5 sec(-1) with (4-nitrophenyl)methanol as substrate (PubMed:25284255).2 Publications
  1. KM=1.4 mM for 5-(hydroxymethyl)furfural1 Publication
  2. KM=1.5 mM for 1,4-benzenedimethanol1 Publication
  3. KM=1.4 mM for 1,3-benzenedimethanol1 Publication
  4. KM=1.3 mM for benzyl alcohol1 Publication
  5. KM=0.3 mM for 4-hydroxybenzyl alcohol1 Publication
  6. KM=1.44 mM for 4-aminobenzyl alcohol1 Publication
  7. KM=0.08 mM for 4-chlorobenzyl alcohol1 Publication
  8. KM=0.07 mM for cinnamyl alcohol1 Publication
  9. KM=0.59 mM for 2,4-hexadien-1-ol1 Publication
  10. KM=0.73 mM for vanillyl alcohol1 Publication
  11. KM=3.5 mM for phenylmethanethiol1 Publication
  12. KM=15 mM for (4-nitrophenyl)methanethiol1 Publication
  13. KM=0.078 mM for (4-nitrophenyl)methanol1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei68FADCombined sources1 Publication1
    Binding sitei94FAD; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei98FAD; via amide nitrogenCombined sources1 Publication1
    Binding sitei233FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
    Binding sitei466FADCombined sources1
    Active sitei467Proton acceptor2 Publications1
    Binding sitei501FAD; via amide nitrogenCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi15 – 16FADCombined sources1 Publication2
    Nucleotide bindingi36 – 37FADCombined sources1 Publication2
    Nucleotide bindingi102 – 105FADCombined sources1 Publication4
    Nucleotide bindingi512 – 513FADCombined sources1 Publication2

    GO - Molecular functioni

    GO - Biological processi

    • oxidation-reduction process Source: UniProtKB

    Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17167
    MSP887061:G1GQ5-130-MONOMER

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-(hydroxymethyl)furfural oxidaseCurated (EC:1.1.3.472 Publications)
    Alternative name(s):
    5-hydroxymethylfurfural oxidase1 Publication
    Short name:
    HMFO1 Publication
    Thiol oxidase1 Publication (EC:1.8.3.-1 Publication)
    Gene namesi
    Ordered Locus Names:MPQ_0130Imported
    OrganismiMethylovorus sp. (strain MP688)
    Taxonomic identifieri887061 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesMethylophilaceaeMethylovorus

    Pathology & Biotechi

    Biotechnological usei

    Because 5-hydroxymethylfurfural can be derived from sugars, the enzyme is of particular interest for the production of biobased plastic materials in an environmentally friendly industrial process.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi101V → H: Abolishes activity. 1 Publication1
    Mutagenesisi103M → A: 16-fold reduction in catalytic efficiency on vanillyl alcohol. 1 Publication1
    Mutagenesisi367V → K: 1.6-fold reduction in catalytic efficiency on vanillyl alcohol. Shows significantly improved activity on the aldehyde 5-formyl-2-furancarboxylate, which results in a better 5-hydroxymethylfurfural to 2,5-furandicarboxylate conversion. 1 Publication1
    Mutagenesisi367V → R: 1.4-fold reduction in catalytic efficiency on vanillyl alcohol. Shows significantly improved activity on the aldehyde 5-formyl-2-furancarboxylate, which results in a better 5-hydroxymethylfurfural to 2,5-furandicarboxylate conversion. Displays a catalytic efficiency toward 5-formyl-2-furancarboxylate that is over 1000-fold higher than that for wild-type; when associated with F-466. 1 Publication1
    Mutagenesisi369W → A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol. 1 Publication1
    Mutagenesisi465V → A: 18-fold reduction in catalytic efficiency on vanillyl alcohol. 1 Publication1
    Mutagenesisi466W → A: 39-fold reduction in catalytic efficiency on vanillyl alcohol. In contrast to wild-type, is active on secondary alcohols, such as (S)-1-phenylethanol, and is strictly enantionselective as this mutant has no activity on (R)-1-phenylethanol. Shows increased activity on the aldehyde 5-formyl-2-furancarboxylate. 1 Publication1
    Mutagenesisi466W → F: 3.4-fold reduction in catalytic efficiency on vanillyl alcohol. In contrast to wild-type, is active on secondary alcohols, such as (S)-1-phenylethanol, and is strictly enantionselective as this mutant has no activity on (R)-1-phenylethanol. Shows increased activity on the aldehyde 5-formyl-2-furancarboxylate. Displays a catalytic efficiency toward 5-formyl-2-furancarboxylate that is over 1000-fold higher than that for wild-type; when associated with R-367. 1 Publication1
    Mutagenesisi467H → A: Abolishes activity. 1 Publication1
    Mutagenesisi511N → A: 53-fold reduction in catalytic efficiency on vanillyl alcohol. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004327101 – 5315-(hydroxymethyl)furfural oxidaseAdd BLAST531

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1531
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 11Combined sources6
    Helixi15 – 25Combined sources11
    Beta strandi32 – 35Combined sources4
    Beta strandi37 – 39Combined sources3
    Helixi43 – 45Combined sources3
    Helixi48 – 51Combined sources4
    Beta strandi52 – 55Combined sources4
    Helixi58 – 61Combined sources4
    Turni63 – 66Combined sources4
    Beta strandi72 – 76Combined sources5
    Turni95 – 97Combined sources3
    Helixi98 – 101Combined sources4
    Helixi111 – 119Combined sources9
    Helixi127 – 137Combined sources11
    Beta strandi138 – 140Combined sources3
    Turni141 – 145Combined sources5
    Beta strandi151 – 158Combined sources8
    Helixi162 – 164Combined sources3
    Helixi167 – 178Combined sources12
    Turni187 – 189Combined sources3
    Beta strandi192 – 196Combined sources5
    Helixi210 – 214Combined sources5
    Helixi217 – 220Combined sources4
    Beta strandi225 – 228Combined sources4
    Beta strandi230 – 239Combined sources10
    Beta strandi242 – 250Combined sources9
    Beta strandi253 – 264Combined sources12
    Turni268 – 270Combined sources3
    Helixi271 – 278Combined sources8
    Helixi283 – 288Combined sources6
    Beta strandi294 – 296Combined sources3
    Turni298 – 301Combined sources4
    Beta strandi303 – 305Combined sources3
    Beta strandi308 – 315Combined sources8
    Helixi318 – 324Combined sources7
    Beta strandi336 – 339Combined sources4
    Beta strandi351 – 358Combined sources8
    Turni359 – 362Combined sources4
    Beta strandi363 – 372Combined sources10
    Beta strandi377 – 380Combined sources4
    Beta strandi382 – 384Combined sources3
    Beta strandi391 – 396Combined sources6
    Helixi400 – 418Combined sources19
    Helixi420 – 423Combined sources4
    Beta strandi430 – 432Combined sources3
    Beta strandi434 – 436Combined sources3
    Helixi444 – 447Combined sources4
    Helixi451 – 461Combined sources11
    Beta strandi488 – 490Combined sources3
    Beta strandi493 – 498Combined sources6
    Helixi501 – 503Combined sources3
    Helixi513 – 528Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4UDPX-ray1.90A/B1-531[»]
    4UDQX-ray1.60A/B1-531[»]
    4UDRX-ray1.60A/B1-531[»]
    6F97X-ray1.90A/B1-531[»]
    SMRiE4QP00
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000139601
    KOiK16873
    OMAiFRTTIRA
    OrthoDBiPOG091H04UT

    Family and domain databases

    Gene3Di3.50.50.60, 4 hits
    InterProiView protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR012132 GMC_OxRdtase
    IPR000172 GMC_OxRdtase_N
    IPR007867 GMC_OxRtase_C
    PfamiView protein in Pfam
    PF05199 GMC_oxred_C, 1 hit
    PF00732 GMC_oxred_N, 1 hit
    PIRSFiPIRSF000137 Alcohol_oxidase, 1 hit
    SUPFAMiSSF51905 SSF51905, 2 hits

    Sequencei

    Sequence statusi: Complete.

    E4QP00-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDTIFDYVI VGGGTAGSVL ANRLSARPEN RVLLIEAGID TPENNIPPEI
    60 70 80 90 100
    HDGLRPWLPR LSGDKFFWPN LTIHRAAEHP GITREPQFYE QGRLLGGGSS
    110 120 130 140 150
    VNMVVSNRGL PRDYDEWQAL GADGWDWQGV LPYFIKTERD ADYGDDPLHG
    160 170 180 190 200
    NAGPIPIGRV DSRHWSDFTV AATQALEAAG LPNIHDQNAR FDDGYFPPAF
    210 220 230 240 250
    TLKGEERFSA ARGYLDASVR VRPNLSLWTE SRVLKLLTTG NAITGVSVLR
    260 270 280 290 300
    GRETLQVQAR EVILTAGALQ SPAILLRTGI GPAADLHALG IPVLADRPGV
    310 320 330 340 350
    GRNLWEHSSI GVVAPLTEQA RADASTGKAG SRHQLGIRAS SGVDPATPSD
    360 370 380 390 400
    LFLHIGADPV SGLASAVFWV NKPSSTGWLK LKDADPFSYP DVDFNLLSDP
    410 420 430 440 450
    RDLGRLKAGL RLITHYFAAP SLAKYGLALA LSRFAAPQPG GPLLNDLLQD
    460 470 480 490 500
    EAALERYLRT NVGGVWHASG TARIGRADDS QAVVDKAGRV YGVTGLRVAD
    510 520 530
    ASIMPTVPTA NTNLPTLMLA EKIADAILTQ A
    Length:531
    Mass (Da):57,014
    Last modified:February 8, 2011 - v1
    Checksum:i111A92125A89F295
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP002252 Genomic DNA Translation: ADQ83320.1
    RefSeqiWP_013440946.1, NC_014733.1

    Genome annotation databases

    EnsemblBacteriaiADQ83320; ADQ83320; MPQ_0130
    KEGGimep:MPQ_0130

    Similar proteinsi

    Entry informationi

    Entry nameiHMFO_METS6
    AccessioniPrimary (citable) accession number: E4QP00
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 2015
    Last sequence update: February 8, 2011
    Last modified: April 25, 2018
    This is version 40 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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

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