Skip Header

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

Aldos-2-ulose dehydratase

Gene
N/A
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

A bifunctional enzyme which catalyzes the dehydration of anhydrofructose into ascopyrone M, and the isomerization of ascopyrone M into microthecin.2 Publications

Catalytic activityi

1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O.3 Publications

Cofactori

Zn2+1 PublicationNote: Binds 3 Zn2+ ions per subunit.1 Publication

Kineticsi

  1. KM=5.4 mM for ascopyrone M1 Publication
  2. KM=7.4 mM for glucosone1 Publication
  3. KM=113 mM for xylosone1 Publication

    pH dependencei

    Optimum pH is 5.8 for dehydration of anhydrofructose and 6.8 for isomerization of ascopyrone M.1 Publication

    Pathwayi: 1,5-anhydro-D-fructose degradation

    This protein is involved in the pathway 1,5-anhydro-D-fructose degradation, which is part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the pathway 1,5-anhydro-D-fructose degradation and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei35Anhydrofructose1 Publication1
    Metal bindingi101Magnesium; structuralCombined sources1 Publication1
    Metal bindingi103Magnesium; structuralCombined sources1 Publication1
    Metal bindingi105Magnesium; structuralCombined sources1 Publication1
    Metal bindingi107Magnesium; via carbonyl oxygen; structuralCombined sources1 Publication1
    Metal bindingi109Magnesium; structuralCombined sources1 Publication1
    Binding sitei116Anhydrofructose1 Publication1
    Binding sitei120Anhydrofructose; via amide nitrogen1 Publication1
    Binding sitei155Anhydrofructose1 Publication1
    Metal bindingi215Zinc 1; via tele nitrogen; catalyticCombined sources1 Publication1
    Metal bindingi295Zinc 1; via tele nitrogen; catalyticCombined sources1 Publication1
    Metal bindingi337Zinc 1; via tele nitrogen; catalyticCombined sources1 Publication1
    Metal bindingi343Zinc 2; structuralCombined sources1 Publication1
    Metal bindingi345Zinc 2; structuralCombined sources1 Publication1
    Metal bindingi347Zinc 2; structuralCombined sources1 Publication1
    Metal bindingi349Zinc 2; via carbonyl oxygen; structuralCombined sources1 Publication1
    Metal bindingi351Zinc 2; structuralCombined sources1 Publication1
    Binding sitei414Anhydrofructose1 Publication1
    Binding sitei419Anhydrofructose1 Publication1
    Binding sitei627Ascopyrone M; via carbonyl oxygen1 Publication1
    Metal bindingi630Zinc 3; via tele nitrogen; catalyticCombined sources1 Publication1
    Metal bindingi632Zinc 3; via tele nitrogen; catalyticCombined sources1 Publication1
    Metal bindingi639Zinc 3; catalyticCombined sources1 Publication1
    Binding sitei641Ascopyrone M1 Publication1
    Metal bindingi709Zinc 3; via tele nitrogen; catalyticCombined sources1 Publication1
    Binding sitei726Ascopyrone M1 Publication1

    GO - Molecular functioni

    • aldos-2-ulose dehydratase activity Source: UniProtKB-EC
    • hydro-lyase activity Source: UniProtKB
    • isomerase activity Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-19294.
    BRENDAi4.2.1.110. 1380.
    5.3.2.7. 1380.
    UniPathwayiUPA00738.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldos-2-ulose dehydratase (EC:4.2.1.1103 Publications)
    Alternative name(s):
    D-arabino-hex-2-ulose dehydratase
    Pyranosone dehydratase
    OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
    Taxonomic identifieri5306 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000647631 – 900Aldos-2-ulose dehydrataseAdd BLAST900

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1900
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi21 – 28Combined sources8
    Beta strandi36 – 40Combined sources5
    Beta strandi42 – 45Combined sources4
    Beta strandi51 – 55Combined sources5
    Beta strandi60 – 62Combined sources3
    Beta strandi64 – 70Combined sources7
    Helixi72 – 74Combined sources3
    Beta strandi75 – 77Combined sources3
    Beta strandi84 – 93Combined sources10
    Beta strandi97 – 100Combined sources4
    Beta strandi105 – 107Combined sources3
    Beta strandi109 – 114Combined sources6
    Beta strandi117 – 119Combined sources3
    Beta strandi129 – 133Combined sources5
    Beta strandi137 – 139Combined sources3
    Beta strandi145 – 150Combined sources6
    Beta strandi154 – 160Combined sources7
    Beta strandi165 – 167Combined sources3
    Beta strandi169 – 175Combined sources7
    Beta strandi186 – 192Combined sources7
    Beta strandi204 – 213Combined sources10
    Beta strandi216 – 220Combined sources5
    Helixi222 – 225Combined sources4
    Beta strandi233 – 238Combined sources6
    Beta strandi241 – 247Combined sources7
    Beta strandi252 – 258Combined sources7
    Beta strandi273 – 280Combined sources8
    Beta strandi283 – 293Combined sources11
    Beta strandi297 – 303Combined sources7
    Beta strandi310 – 312Combined sources3
    Beta strandi318 – 324Combined sources7
    Beta strandi335 – 342Combined sources8
    Beta strandi346 – 349Combined sources4
    Beta strandi351 – 357Combined sources7
    Helixi364 – 366Combined sources3
    Beta strandi367 – 376Combined sources10
    Turni377 – 380Combined sources4
    Beta strandi381 – 388Combined sources8
    Beta strandi393 – 398Combined sources6
    Beta strandi401 – 405Combined sources5
    Beta strandi408 – 412Combined sources5
    Turni417 – 419Combined sources3
    Beta strandi427 – 439Combined sources13
    Beta strandi441 – 448Combined sources8
    Helixi451 – 453Combined sources3
    Beta strandi458 – 465Combined sources8
    Beta strandi468 – 475Combined sources8
    Beta strandi480 – 482Combined sources3
    Turni485 – 487Combined sources3
    Beta strandi489 – 501Combined sources13
    Beta strandi504 – 508Combined sources5
    Beta strandi517 – 519Combined sources3
    Beta strandi524 – 541Combined sources18
    Beta strandi543 – 545Combined sources3
    Helixi553 – 556Combined sources4
    Helixi568 – 571Combined sources4
    Helixi580 – 582Combined sources3
    Turni587 – 592Combined sources6
    Beta strandi595 – 605Combined sources11
    Beta strandi612 – 621Combined sources10
    Beta strandi638 – 645Combined sources8
    Beta strandi647 – 649Combined sources3
    Beta strandi652 – 656Combined sources5
    Helixi660 – 662Combined sources3
    Beta strandi665 – 667Combined sources3
    Helixi670 – 672Combined sources3
    Beta strandi673 – 677Combined sources5
    Beta strandi682 – 684Combined sources3
    Beta strandi708 – 712Combined sources5
    Beta strandi724 – 731Combined sources8
    Beta strandi749 – 757Combined sources9
    Beta strandi760 – 766Combined sources7
    Helixi767 – 769Combined sources3
    Beta strandi775 – 781Combined sources7
    Beta strandi792 – 796Combined sources5
    Beta strandi803 – 807Combined sources5
    Turni808 – 810Combined sources3
    Beta strandi813 – 816Combined sources4
    Beta strandi824 – 831Combined sources8
    Helixi834 – 836Combined sources3
    Turni837 – 839Combined sources3
    Beta strandi841 – 845Combined sources5
    Beta strandi851 – 854Combined sources4
    Beta strandi859 – 861Combined sources3
    Beta strandi865 – 869Combined sources5
    Beta strandi879 – 887Combined sources9
    Helixi889 – 892Combined sources4
    Beta strandi894 – 898Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4A7KX-ray2.00A1-900[»]
    4A7YX-ray2.80A1-900[»]
    4A7ZX-ray2.60A1-900[»]
    SMRiP84193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 433Dehydratase domain1 PublicationAdd BLAST433
    Regioni434 – 739Isomerase domain1 PublicationAdd BLAST306

    Sequencei

    Sequence statusi: Complete.

    P84193-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYSKVFLKPH CEPEQPAALP LFQPQLVQGG RPDGYWVEAF PFRSDSSKCP
    60 70 80 90 100
    NIIGYGLGTY DMKSDIQMLV NPYATTNNQS SSWTPVPLAK LDFPVAMHYA
    110 120 130 140 150
    DITKNGFNDV IITDQYGSSM DDIWAYGGRV SWLENPGELR DNWTMRTIGH
    160 170 180 190 200
    SPGMHRLKAG HFTRTDRVQV VAVPIVVASS DLTTPADVII FTAPDDPRSE
    210 220 230 240 250
    QLWQRDVVGT RHLVHEVAIV PAAETDGEMR FDQIILAGRD GVDCLWYDGA
    260 270 280 290 300
    RWQRHLVGTG LPEERGDPYW GAGSAAVGRV GDDYAGYICS AEAFHGNTVS
    310 320 330 340 350
    VYTKPAGSPT GIVRAEWTRH VLDVFGPLNG KHTGSIHQVV CADIDGDGED
    360 370 380 390 400
    EFLVAMMGAD PPDFQRTGVW CYKLVDRTNM KFSKTKVSSV SAGRIATANF
    410 420 430 440 450
    HSQGSEVDIA TISYSVPGYF ESPNPSINVF LSTGILAERL DEEVMLRVVR
    460 470 480 490 500
    AGSTRFKTEM EFLDVAGKKL TLVVLPPFAR LDVERNVSGV KVMAGTVCWA
    510 520 530 540 550
    DENGKHERVP ATRPFGCESM IVSADYLESG EEGAILVLYK PSSTSGRPPF
    560 570 580 590 600
    RSMDELVAHN LFPAYVPDSV RAMKFPWVRC ADRPWAHGRF KDLDFFNLIG
    610 620 630 640 650
    FHVNFADDSA AVLAHVQLWT AGIGVSAGFH NHVEASFCEI HACIANGTGR
    660 670 680 690 700
    GGMRWATVPD ANFNPDSPNL EDTELIVVPD MHEHGPLWRT RPDGHPLLRM
    710 720 730 740 750
    NDTIDYPWHA WLAGAGNPSP QAFDVWVAFE FPGFETFSTP PPPRVLEPGR
    760 770 780 790 800
    YAIRFGDPHQ TASLALQKND ATDGTPVLAL LDLDGGPSPQ AWNISHVPGT
    810 820 830 840 850
    DMYEIAHAKT GSLVCARWPP VKNQRVAGTH SPAAMGLTSR WAVTKNTKGQ
    860 870 880 890 900
    ITFRLPEAPD HGPLFLSVSA IRHQQEADAI PVIVQGDSIE LSAWSLVPAN
    Length:900
    Mass (Da):98,746
    Last modified:January 25, 2012 - v3
    Checksum:i9940933835C52113
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti69L → F in AGY31289 (Ref. 2) Curated1
    Sequence conflicti69L → F AA sequence (PubMed:15716041).Curated1
    Sequence conflicti87P → S in AGY31289 (Ref. 2) Curated1
    Sequence conflicti87P → S AA sequence (PubMed:15716041).Curated1
    Sequence conflicti254R → K in AGY31289 (Ref. 2) Curated1
    Sequence conflicti798P → PP AA sequence (PubMed:15716041).Curated1
    Sequence conflicti876E → G in AGY31289 (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    KF699142 mRNA. Translation: AGY31289.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    KF699142 mRNA. Translation: AGY31289.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4A7KX-ray2.00A1-900[»]
    4A7YX-ray2.80A1-900[»]
    4A7ZX-ray2.60A1-900[»]
    SMRiP84193.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00738.
    BioCyciMetaCyc:MONOMER-19294.
    BRENDAi4.2.1.110. 1380.
    5.3.2.7. 1380.

    Family and domain databases

    ProtoNetiSearch...

    Entry informationi

    Entry nameiAUD_PHACH
    AccessioniPrimary (citable) accession number: P84193
    Secondary accession number(s): U5NJV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: January 25, 2012
    Last modified: November 2, 2016
    This is version 30 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme

    Documents

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

    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.