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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351Anhydrofructose1 Publication
    Metal bindingi101 – 1011Magnesium; structuralCombined sources1 Publication
    Metal bindingi103 – 1031Magnesium; structuralCombined sources1 Publication
    Metal bindingi105 – 1051Magnesium; structuralCombined sources1 Publication
    Metal bindingi107 – 1071Magnesium; via carbonyl oxygen; structuralCombined sources1 Publication
    Metal bindingi109 – 1091Magnesium; structuralCombined sources1 Publication
    Binding sitei116 – 1161Anhydrofructose1 Publication
    Binding sitei120 – 1201Anhydrofructose; via amide nitrogen1 Publication
    Binding sitei155 – 1551Anhydrofructose1 Publication
    Metal bindingi215 – 2151Zinc 1; via tele nitrogen; catalyticCombined sources1 Publication
    Metal bindingi295 – 2951Zinc 1; via tele nitrogen; catalyticCombined sources1 Publication
    Metal bindingi337 – 3371Zinc 1; via tele nitrogen; catalyticCombined sources1 Publication
    Metal bindingi343 – 3431Zinc 2; structuralCombined sources1 Publication
    Metal bindingi345 – 3451Zinc 2; structuralCombined sources1 Publication
    Metal bindingi347 – 3471Zinc 2; structuralCombined sources1 Publication
    Metal bindingi349 – 3491Zinc 2; via carbonyl oxygen; structuralCombined sources1 Publication
    Metal bindingi351 – 3511Zinc 2; structuralCombined sources1 Publication
    Binding sitei414 – 4141Anhydrofructose1 Publication
    Binding sitei419 – 4191Anhydrofructose1 Publication
    Binding sitei627 – 6271Ascopyrone M; via carbonyl oxygen1 Publication
    Metal bindingi630 – 6301Zinc 3; via tele nitrogen; catalyticCombined sources1 Publication
    Metal bindingi632 – 6321Zinc 3; via tele nitrogen; catalyticCombined sources1 Publication
    Metal bindingi639 – 6391Zinc 3; catalyticCombined sources1 Publication
    Binding sitei641 – 6411Ascopyrone M1 Publication
    Metal bindingi709 – 7091Zinc 3; via tele nitrogen; catalyticCombined sources1 Publication
    Binding sitei726 – 7261Ascopyrone M1 Publication

    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

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Aldos-2-ulose dehydratasePRO_0000064763Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    900
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 288Combined sources
    Beta strandi36 – 405Combined sources
    Beta strandi42 – 454Combined sources
    Beta strandi51 – 555Combined sources
    Beta strandi60 – 623Combined sources
    Beta strandi64 – 707Combined sources
    Helixi72 – 743Combined sources
    Beta strandi75 – 773Combined sources
    Beta strandi84 – 9310Combined sources
    Beta strandi97 – 1004Combined sources
    Beta strandi105 – 1073Combined sources
    Beta strandi109 – 1146Combined sources
    Beta strandi117 – 1193Combined sources
    Beta strandi129 – 1335Combined sources
    Beta strandi137 – 1393Combined sources
    Beta strandi145 – 1506Combined sources
    Beta strandi154 – 1607Combined sources
    Beta strandi165 – 1673Combined sources
    Beta strandi169 – 1757Combined sources
    Beta strandi186 – 1927Combined sources
    Beta strandi204 – 21310Combined sources
    Beta strandi216 – 2205Combined sources
    Helixi222 – 2254Combined sources
    Beta strandi233 – 2386Combined sources
    Beta strandi241 – 2477Combined sources
    Beta strandi252 – 2587Combined sources
    Beta strandi273 – 2808Combined sources
    Beta strandi283 – 29311Combined sources
    Beta strandi297 – 3037Combined sources
    Beta strandi310 – 3123Combined sources
    Beta strandi318 – 3247Combined sources
    Beta strandi335 – 3428Combined sources
    Beta strandi346 – 3494Combined sources
    Beta strandi351 – 3577Combined sources
    Helixi364 – 3663Combined sources
    Beta strandi367 – 37610Combined sources
    Turni377 – 3804Combined sources
    Beta strandi381 – 3888Combined sources
    Beta strandi393 – 3986Combined sources
    Beta strandi401 – 4055Combined sources
    Beta strandi408 – 4125Combined sources
    Turni417 – 4193Combined sources
    Beta strandi427 – 43913Combined sources
    Beta strandi441 – 4488Combined sources
    Helixi451 – 4533Combined sources
    Beta strandi458 – 4658Combined sources
    Beta strandi468 – 4758Combined sources
    Beta strandi480 – 4823Combined sources
    Turni485 – 4873Combined sources
    Beta strandi489 – 50113Combined sources
    Beta strandi504 – 5085Combined sources
    Beta strandi517 – 5193Combined sources
    Beta strandi524 – 54118Combined sources
    Beta strandi543 – 5453Combined sources
    Helixi553 – 5564Combined sources
    Helixi568 – 5714Combined sources
    Helixi580 – 5823Combined sources
    Turni587 – 5926Combined sources
    Beta strandi595 – 60511Combined sources
    Beta strandi612 – 62110Combined sources
    Beta strandi638 – 6458Combined sources
    Beta strandi647 – 6493Combined sources
    Beta strandi652 – 6565Combined sources
    Helixi660 – 6623Combined sources
    Beta strandi665 – 6673Combined sources
    Helixi670 – 6723Combined sources
    Beta strandi673 – 6775Combined sources
    Beta strandi682 – 6843Combined sources
    Beta strandi708 – 7125Combined sources
    Beta strandi724 – 7318Combined sources
    Beta strandi749 – 7579Combined sources
    Beta strandi760 – 7667Combined sources
    Helixi767 – 7693Combined sources
    Beta strandi775 – 7817Combined sources
    Beta strandi792 – 7965Combined sources
    Beta strandi803 – 8075Combined sources
    Turni808 – 8103Combined sources
    Beta strandi813 – 8164Combined sources
    Beta strandi824 – 8318Combined sources
    Helixi834 – 8363Combined sources
    Turni837 – 8393Combined sources
    Beta strandi841 – 8455Combined sources
    Beta strandi851 – 8544Combined sources
    Beta strandi859 – 8613Combined sources
    Beta strandi865 – 8695Combined sources
    Beta strandi879 – 8879Combined sources
    Helixi889 – 8924Combined sources
    Beta strandi894 – 8985Combined sources

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 433433Dehydratase domain1 PublicationAdd
    BLAST
    Regioni434 – 739306Isomerase domain1 PublicationAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691L → F in AGY31289 (Ref. 2) Curated
    Sequence conflicti69 – 691L → F AA sequence (PubMed:15716041).Curated
    Sequence conflicti87 – 871P → S in AGY31289 (Ref. 2) Curated
    Sequence conflicti87 – 871P → S AA sequence (PubMed:15716041).Curated
    Sequence conflicti254 – 2541R → K in AGY31289 (Ref. 2) Curated
    Sequence conflicti798 – 7981P → PP AA sequence (PubMed:15716041).Curated
    Sequence conflicti876 – 8761E → G in AGY31289 (Ref. 2) Curated

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A7KX-ray2.00A1-900[»]
    4A7YX-ray2.80A1-900[»]
    4A7ZX-ray2.60A1-900[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00738.
    BRENDAi4.2.1.110. 1380.
    5.3.2.7. 1380.

    Family and domain databases

    ProtoNetiSearch...

    Publicationsi

    1. "Crystal structure of bifunctional aldos-2-ulose dehydratase/isomerase from Phanerochaete chrysosporium with the reaction intermediate ascopyrone M."
      Claesson M., Lindqvist Y., Madrid S., Sandalova T., Fiskesund R., Yu S., Schneider G.
      J. Mol. Biol. 417:279-293(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH 1,5-ANHYDRO-D-FRUCTOSE; ASCOPYRONE M; ZINC AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 32629 / DSM 1547 / CBS 246.84 / BCRC 36201.
    2. "Integration of chemical and biological catalysis: production of furylglycolic acid from glucose via cortalcerone."
      Schwartz T., Goodman S., Osmundsen C., Taarning E., Mozuch M., Gaskell J., Cullen D., Kersten P., Dumesic J.A.
      ACS Catal. 3:2689-2693(2013)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
      Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767Imported.
    3. "Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-d-fructose to microthecin with ascopyrone M as the intermediate."
      Yu S.
      Biochim. Biophys. Acta 1723:63-73(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-48; 64-104; 130-141; 241-251; 305-337; 338-373; 458-491; 552-571; 769-845 AND 849-874, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 32629 / DSM 1547 / CBS 246.84 / BCRC 36201.

    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: July 6, 2016
    This is version 29 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.