ARD1_UROFA
ID ARD1_UROFA Reviewed; 349 AA.
AC Q4R0J7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=D-arabinitol dehydrogenase 1;
DE EC=1.1.1.287;
DE AltName: Full=NADP-dependent D-arabitol dehydrogenase;
GN Name=ARD1;
OS Uromyces fabae (Rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces.
OX NCBI_TaxID=55588;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=15796718; DOI=10.1042/bj20050301;
RA Link T., Lohaus G., Heiser I., Mendgen K., Hahn M., Voegele R.T.;
RT "Characterization of a novel NADP(+)-dependent D-arabitol dehydrogenase
RT from the plant pathogen Uromyces fabae.";
RL Biochem. J. 389:289-295(2005).
CC -!- FUNCTION: D-arabinitol dehydrogenase which mostly produces D-arabinitol
CC in haustoria, the appendages of the parasitic fungus that penetrate the
CC host's tissue and draws nutrients from it. D-arabinitol accumulation
CC may serve as a carbohydrate storage compound. D-arabinitol is also
CC capable of quenching reactive oxygen species involved in host plant
CC defense reactions, thus providing protection for the rust fungus during
CC the pathogenic interaction. {ECO:0000269|PubMed:15796718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinitol + NADP(+) = D-xylulose + H(+) + NADPH;
CC Xref=Rhea:RHEA:21276, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:18333, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.287; Evidence={ECO:0000269|PubMed:15796718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinitol + NADP(+) = D-ribulose + H(+) + NADPH;
CC Xref=Rhea:RHEA:11868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:18333, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.287; Evidence={ECO:0000269|PubMed:15796718};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=706 mM for D-arabinitol {ECO:0000269|PubMed:15796718};
CC KM=150 uM for NADP {ECO:0000269|PubMed:15796718};
CC Vmax=117 nmol/min/mg enzyme toward D-arabinitol
CC {ECO:0000269|PubMed:15796718};
CC Vmax=97 nmol/min/mg enzyme toward NADP {ECO:0000269|PubMed:15796718};
CC pH dependence:
CC Optimum pH is 9 for the forward reaction, and 6 for the reverse
CC reaction. {ECO:0000269|PubMed:15796718};
CC -!- SUBCELLULAR LOCATION: Cell projection. Note=Localizes in the lumen of
CC haustoria.
CC -!- INDUCTION: Expressed at all stages of early rust development (spores,
CC germlings and infection structures developed on an artificial surface),
CC with highest transcript levels present in haustoria.
CC {ECO:0000269|PubMed:15796718}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ809335; CAH10835.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4R0J7; -.
DR SMR; Q4R0J7; -.
DR KEGG; ag:CAH10835; -.
DR BRENDA; 1.1.1.287; 6579.
DR SABIO-RK; Q4R0J7; -.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0033709; F:D-arabinitol dehydrogenase, D-ribulose forming (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0052677; F:D-arabinitol dehydrogenase, D-xylulose forming (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell projection; Metal-binding; NADP;
KW Oxidoreductase; Virulence; Zinc.
FT CHAIN 1..349
FT /note="D-arabinitol dehydrogenase 1"
FT /id="PRO_0000418402"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 38372 MW; A16F1C5C6A0456AB CRC64;
MATQTLPAQM TALYYEKPRD FSIIKADVPL IDHDEVLLKV SMCGVCGTDQ HIHEGEFIAK
FPLIPGHEVI GTIVLAGNQV ENVKVGDRVV CDVSETCHKC FFCQRGTPLF CESFEAHGVT
LNGGFAEYAK FRAAKVFPIK NLTDEQATLV EPASCAVHGL DKIRPKPGSE CLLIGAGPTG
LMLAQLLKLN GAQRVVLAAN KGMKMDIARK INAADEYIDL DRKDAANQWA QLKEDNPHGF
DVVVEATGVE SIVNDSINYV RRGGTLLVYG VYDNAARVTW SPTKIFQDEI NIVGSFAQIH
CFPRAVAYLE SGKIRTDGMV THVYKIEEYQ EALDKMASRQ CLKIAVKPN
