PERR_RAUSE
ID PERR_RAUSE Reviewed; 337 AA.
AC Q3L181;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Perakine reductase;
DE EC=1.1.1.317;
GN Name=PR;
OS Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Rauvolfiinae; Rauvolfia.
OX NCBI_TaxID=4060;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-52; TYR-57; LYS-84 AND
RP HIS-126, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18409028; DOI=10.1007/s11103-008-9331-7;
RA Sun L., Ruppert M., Sheludko Y., Warzecha H., Zhao Y., Stockigt J.;
RT "Purification, cloning, functional expression and characterization of
RT perakine reductase: the first example from the AKR enzyme family, extending
RT the alkaloidal network of the plant Rauvolfia.";
RL Plant Mol. Biol. 67:455-467(2008).
RN [2]
RP CRYSTALLIZATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17142919; DOI=10.1107/s174430910605041x;
RA Rosenthal C., Mueller U., Panjikar S., Sun L., Ruppert M., Zhao Y.,
RA Stockigt J.;
RT "Expression, purification, crystallization and preliminary X-ray analysis
RT of perakine reductase, a new member of the aldo-keto reductase enzyme
RT superfamily from higher plants.";
RL Acta Crystallogr. F 62:1286-1289(2006).
CC -!- FUNCTION: Aldo-keto reductase involved in the biosynthesis of
CC monoterpenoid indole alkaloids. Broad substrate specificity enzyme with
CC a high selectivity in the group of alkaloids. Can use perakine,
CC 19(S),20(R)-dihydro-peraksine-17,21-al, cinnamic aldehyde, p-coumaric
CC aldehyde and 3-(3,4,5-trimethoxyphenyl)propanal as substrates, but not
CC ketosteroids such as progesterone. NADPH could not be replaced by NADH.
CC {ECO:0000269|PubMed:18409028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + raucaffrinoline = H(+) + NADPH + perakine;
CC Xref=Rhea:RHEA:31675, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:63167, ChEBI:CHEBI:63168;
CC EC=1.1.1.317; Evidence={ECO:0000269|PubMed:17142919,
CC ECO:0000269|PubMed:18409028};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for 4-nitrobenzaldehyde {ECO:0000269|PubMed:17142919,
CC ECO:0000269|PubMed:18409028};
CC KM=0.83 mM for perakine {ECO:0000269|PubMed:17142919,
CC ECO:0000269|PubMed:18409028};
CC KM=1.29 mM for coniferyl aldehyde {ECO:0000269|PubMed:17142919,
CC ECO:0000269|PubMed:18409028};
CC Vmax=217.39 pmol/sec/ug enzyme with 4-nitrobenzaldehyde as substrate
CC {ECO:0000269|PubMed:17142919, ECO:0000269|PubMed:18409028};
CC Vmax=0.368 pmol/sec/ug enzyme with perakine as substrate
CC {ECO:0000269|PubMed:17142919, ECO:0000269|PubMed:18409028};
CC Vmax=1.11 pmol/sec/ug enzyme with coniferyl aldehyde as substrate
CC {ECO:0000269|PubMed:17142919, ECO:0000269|PubMed:18409028};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17142919,
CC ECO:0000269|PubMed:18409028};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:17142919, ECO:0000269|PubMed:18409028};
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AY766462; AAX11684.1; -; mRNA.
DR PDB; 3UYI; X-ray; 2.31 A; A=1-336.
DR PDB; 3V0S; X-ray; 1.77 A; A=1-337.
DR PDB; 3V0T; X-ray; 2.33 A; A=1-337.
DR PDB; 3V0U; X-ray; 2.20 A; A=1-337.
DR PDBsum; 3UYI; -.
DR PDBsum; 3V0S; -.
DR PDBsum; 3V0T; -.
DR PDBsum; 3V0U; -.
DR AlphaFoldDB; Q3L181; -.
DR SMR; Q3L181; -.
DR KEGG; ag:AAX11684; -.
DR BioCyc; MetaCyc:MONMETA-16871; -.
DR BRENDA; 1.1.1.317; 5309.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alkaloid metabolism; NADP; Oxidoreductase.
FT CHAIN 1..337
FT /note="Perakine reductase"
FT /id="PRO_0000415739"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MUTAGEN 52
FT /note="D->A: 99% loss of activity."
FT /evidence="ECO:0000269|PubMed:18409028"
FT MUTAGEN 57
FT /note="Y->A: 99% loss of activity."
FT /evidence="ECO:0000269|PubMed:18409028"
FT MUTAGEN 84
FT /note="K->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:18409028"
FT MUTAGEN 126
FT /note="H->A: 98% loss of activity."
FT /evidence="ECO:0000269|PubMed:18409028"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3V0U"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:3V0S"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3V0S"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3V0S"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:3UYI"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:3UYI"
SQ SEQUENCE 337 AA; 37160 MW; 109BE344F4A7D7FD CRC64;
MPRVKLGTQG LEVSKLGFGC MGLSGDYNDA LPEEQGIAVI KEAFNCGITF FDTSDIYGEN
GSNEELLGKA LKQLPREKIQ VGTKFGIHEI GFSGVKAKGT PDYVRSCCEA SLKRLDVDYI
DLFYIHRIDT TVPIEITMGE LKKLVEEGKI KYVGLSEASP DTIRRAHAVH PVTALQIEYS
LWTRDIEDEI VPLCRQLGIG IVPYSPIGRG LFAGKAIKES LPENSVLTSH PRFVGENLEK
NKQIYYRIEA LSQKHGCTPV QLALAWVLHQ GEDVVPIPGT TKIKNLHNNV GALKVKLTKE
DLKEISDAVP LDEVAGESIH EVIAVTNWKF ANTPPLK
