ID   IFRH_MAIZE              Reviewed;         309 AA.
AC   P52580;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Isoflavone reductase homolog IRL {ECO:0000303|PubMed:8597660};
DE            EC=1.3.1.- {ECO:0000250|UniProtKB:P52579};
GN   Name=IRL {ECO:0000303|PubMed:8597660};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INDUCTION BY SULFUR DEPRIVATION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Dekalb XL72;
RX   PubMed=8597660; DOI=10.2307/3870069;
RA   Petrucco S., Bolchi A., Foroni C., Percudani R., Rossi G.L., Ottonello S.;
RT   "A maize gene encoding an NADPH binding enzyme highly homologous to
RT   isoflavone reductases is activated in response to sulfur starvation.";
RL   Plant Cell 8:69-80(1996).
CC   -!- FUNCTION: Reductase that may be involved in a late step of alkaloid
CC       biosynthesis. {ECO:0000250|UniProtKB:P52579}.
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:B7UEU8}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8597660}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8597660}.
CC   -!- INDUCTION: By sulfur deprivation.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; U33318; AAC49210.1; -; mRNA.
DR   PIR; T02304; T02304.
DR   AlphaFoldDB; P52580; -.
DR   SMR; P52580; -.
DR   STRING; 4577.AC226235.2_FGP001; -.
DR   PaxDb; P52580; -.
DR   PRIDE; P52580; -.
DR   MaizeGDB; 123916; -.
DR   eggNOG; ENOG502QPMY; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P52580; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070402; F:NADPH binding; IDA:AgBase.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010438; P:cellular response to sulfur starvation; IEP:AgBase.
DR   CDD; cd05259; PCBER_SDR_a; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   InterPro; IPR045312; PCBER-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Cytoplasm; NADP; Oxidoreductase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..309
FT                   /note="Isoflavone reductase homolog IRL"
FT                   /id="PRO_0000204549"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         12..18
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         46
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         138
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ   SEQUENCE   309 AA;  32852 MW;  138314D67B16BA5B CRC64;
     MASEKSKILV VGGTGYLGRH VVAASARLGH PTSALVRDTA PSDPAKAALL KSFQDAGVTL
     LKGDLYDQAS LVSAVKGADV VISVLGSMQI ADQSRLVDAI KEAGNVKRFF PSEFGLDVDR
     TGIVEPAKSI LGAKVGIRRA TEAAGIPYTY AVAGFFAGFG LPKVGQVLAP GPPADKAVVL
     GDGDTKAVFV EEGDIATYTV LAADDPRAEN KVLYIKPPAN TLSHNELLSL WEKKTGKTFR
     REYVPEEAVL KQIQESPIPL NIILAIGHAA FVRGEQTGFE IDPAKGVDAS ELYPDVKYTT
     VDEYLNRFL