AUD_PHACH
ID AUD_PHACH Reviewed; 900 AA.
AC P84193; U5NJV3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Aldos-2-ulose dehydratase;
DE EC=4.2.1.110 {ECO:0000269|PubMed:15716041, ECO:0000269|PubMed:22330145, ECO:0000269|Ref.2};
DE AltName: Full=D-arabino-hex-2-ulose dehydratase;
DE AltName: Full=Pyranosone dehydratase;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES
RP WITH 1,5-ANHYDRO-D-FRUCTOSE; ASCOPYRONE M; ZINC AND MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 32629 / DSM 1547 / CBS 246.84 / BCRC 36201;
RX PubMed=22330145; DOI=10.1016/j.jmb.2012.02.001;
RA Claesson M., Lindqvist Y., Madrid S., Sandalova T., Fiskesund R., Yu S.,
RA Schneider G.;
RT "Crystal structure of bifunctional aldos-2-ulose dehydratase/isomerase from
RT Phanerochaete chrysosporium with the reaction intermediate ascopyrone M.";
RL J. Mol. Biol. 417:279-293(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767 {ECO:0000312|EMBL:AGY31289.1};
RA Schwartz T., Goodman S., Osmundsen C., Taarning E., Mozuch M., Gaskell J.,
RA Cullen D., Kersten P., Dumesic J.A.;
RT "Integration of chemical and biological catalysis: production of
RT furylglycolic acid from glucose via cortalcerone.";
RL ACS Catal. 3:2689-2693(2013).
RN [3]
RP PROTEIN SEQUENCE OF 8-48; 64-104; 130-141; 241-251; 305-337; 338-373;
RP 458-491; 552-571; 769-845 AND 849-874, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 32629 / DSM 1547 / CBS 246.84 / BCRC 36201;
RX PubMed=15716041; DOI=10.1016/j.bbagen.2005.01.004;
RA Yu S.;
RT "Enzymatic description of the anhydrofructose pathway of glycogen
RT degradation II. Gene identification and characterization of the reactions
RT catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-d-fructose
RT to microthecin with ascopyrone M as the intermediate.";
RL Biochim. Biophys. Acta 1723:63-73(2005).
CC -!- FUNCTION: A bifunctional enzyme which catalyzes the dehydration of
CC anhydrofructose into ascopyrone M, and the isomerization of ascopyrone
CC M into microthecin. {ECO:0000269|PubMed:15716041,
CC ECO:0000269|PubMed:22330145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,5-anhydro-D-fructose = H2O + microthecin;
CC Xref=Rhea:RHEA:12100, ChEBI:CHEBI:15377, ChEBI:CHEBI:16715,
CC ChEBI:CHEBI:51835; EC=4.2.1.110;
CC Evidence={ECO:0000269|PubMed:15716041, ECO:0000269|PubMed:22330145,
CC ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22330145};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000269|PubMed:22330145};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 mM for ascopyrone M {ECO:0000269|PubMed:22330145};
CC KM=7.4 mM for glucosone {ECO:0000269|PubMed:22330145};
CC KM=113 mM for xylosone {ECO:0000269|PubMed:22330145};
CC pH dependence:
CC Optimum pH is 5.8 for dehydration of anhydrofructose and 6.8 for
CC isomerization of ascopyrone M. {ECO:0000269|PubMed:15716041};
CC -!- PATHWAY: Carbohydrate metabolism; 1,5-anhydro-D-fructose degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:22330145}.
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DR EMBL; KF699142; AGY31289.1; -; mRNA.
DR PDB; 4A7K; X-ray; 2.00 A; A=1-900.
DR PDB; 4A7Y; X-ray; 2.80 A; A=1-900.
DR PDB; 4A7Z; X-ray; 2.60 A; A=1-900.
DR PDBsum; 4A7K; -.
DR PDBsum; 4A7Y; -.
DR PDBsum; 4A7Z; -.
DR AlphaFoldDB; P84193; -.
DR SMR; P84193; -.
DR KEGG; ag:AGY31289; -.
DR VEuPathDB; FungiDB:AGR57_3658; -.
DR BioCyc; MetaCyc:MON-19294; -.
DR BRENDA; 4.2.1.110; 1380.
DR BRENDA; 5.3.2.7; 1380.
DR UniPathway; UPA00738; -.
DR GO; GO:0033991; F:aldos-2-ulose dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0016853; F:isomerase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR040887; AUDH_Cupin.
DR InterPro; IPR028994; Integrin_alpha_N.
DR Pfam; PF18637; AUDH_Cupin; 1.
DR SUPFAM; SSF69318; SSF69318; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Lyase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Zinc.
FT CHAIN 1..900
FT /note="Aldos-2-ulose dehydratase"
FT /id="PRO_0000064763"
FT REGION 1..433
FT /note="Dehydratase domain"
FT /evidence="ECO:0000303|PubMed:22330145"
FT REGION 434..739
FT /note="Isomerase domain"
FT /evidence="ECO:0000303|PubMed:22330145"
FT BINDING 35
FT /ligand="1,5-anhydro-D-fructose"
FT /ligand_id="ChEBI:CHEBI:16715"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 116
FT /ligand="1,5-anhydro-D-fructose"
FT /ligand_id="ChEBI:CHEBI:16715"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 120
FT /ligand="1,5-anhydro-D-fructose"
FT /ligand_id="ChEBI:CHEBI:16715"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 155
FT /ligand="1,5-anhydro-D-fructose"
FT /ligand_id="ChEBI:CHEBI:16715"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 414
FT /ligand="1,5-anhydro-D-fructose"
FT /ligand_id="ChEBI:CHEBI:16715"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 419
FT /ligand="1,5-anhydro-D-fructose"
FT /ligand_id="ChEBI:CHEBI:16715"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 627
FT /ligand="ascopyrone M"
FT /ligand_id="ChEBI:CHEBI:50070"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 639
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 641
FT /ligand="ascopyrone M"
FT /ligand_id="ChEBI:CHEBI:50070"
FT /evidence="ECO:0000305|PubMed:22330145"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22330145,
FT ECO:0007744|PDB:4A7K"
FT BINDING 726
FT /ligand="ascopyrone M"
FT /ligand_id="ChEBI:CHEBI:50070"
FT /evidence="ECO:0000305|PubMed:22330145"
FT CONFLICT 69
FT /note="L -> F (in Ref. 2; AGY31289 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="P -> S (in Ref. 2; AGY31289 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> K (in Ref. 2; AGY31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="P -> PP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="E -> G (in Ref. 2; AGY31289)"
FT /evidence="ECO:0000305"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4A7Z"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4A7Z"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4A7Z"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4A7Z"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:4A7K"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:4A7K"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 427..439
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 441..448
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:4A7K"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 489..501
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 524..541
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 553..556
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:4A7K"
FT TURN 587..592
FT /evidence="ECO:0007829|PDB:4A7Y"
FT STRAND 595..605
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 612..621
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 652..656
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:4A7Y"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 673..677
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 724..731
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 749..757
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 760..766
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 775..781
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 792..796
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:4A7K"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 824..831
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:4A7K"
FT TURN 837..839
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 841..845
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 865..869
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 879..887
FT /evidence="ECO:0007829|PDB:4A7K"
FT HELIX 889..892
FT /evidence="ECO:0007829|PDB:4A7K"
FT STRAND 894..898
FT /evidence="ECO:0007829|PDB:4A7K"
SQ SEQUENCE 900 AA; 98746 MW; 9940933835C52113 CRC64;
MYSKVFLKPH CEPEQPAALP LFQPQLVQGG RPDGYWVEAF PFRSDSSKCP NIIGYGLGTY
DMKSDIQMLV NPYATTNNQS SSWTPVPLAK LDFPVAMHYA DITKNGFNDV IITDQYGSSM
DDIWAYGGRV SWLENPGELR DNWTMRTIGH SPGMHRLKAG HFTRTDRVQV VAVPIVVASS
DLTTPADVII FTAPDDPRSE QLWQRDVVGT RHLVHEVAIV PAAETDGEMR FDQIILAGRD
GVDCLWYDGA RWQRHLVGTG LPEERGDPYW GAGSAAVGRV GDDYAGYICS AEAFHGNTVS
VYTKPAGSPT GIVRAEWTRH VLDVFGPLNG KHTGSIHQVV CADIDGDGED EFLVAMMGAD
PPDFQRTGVW CYKLVDRTNM KFSKTKVSSV SAGRIATANF HSQGSEVDIA TISYSVPGYF
ESPNPSINVF LSTGILAERL DEEVMLRVVR AGSTRFKTEM EFLDVAGKKL TLVVLPPFAR
LDVERNVSGV KVMAGTVCWA DENGKHERVP ATRPFGCESM IVSADYLESG EEGAILVLYK
PSSTSGRPPF RSMDELVAHN LFPAYVPDSV RAMKFPWVRC ADRPWAHGRF KDLDFFNLIG
FHVNFADDSA AVLAHVQLWT AGIGVSAGFH NHVEASFCEI HACIANGTGR GGMRWATVPD
ANFNPDSPNL EDTELIVVPD MHEHGPLWRT RPDGHPLLRM NDTIDYPWHA WLAGAGNPSP
QAFDVWVAFE FPGFETFSTP PPPRVLEPGR YAIRFGDPHQ TASLALQKND ATDGTPVLAL
LDLDGGPSPQ AWNISHVPGT DMYEIAHAKT GSLVCARWPP VKNQRVAGTH SPAAMGLTSR
WAVTKNTKGQ ITFRLPEAPD HGPLFLSVSA IRHQQEADAI PVIVQGDSIE LSAWSLVPAN
