I3ACR_SCHPO
ID I3ACR_SCHPO Reviewed; 284 AA.
AC O13848;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=NAD/NADP-dependent indole-3-acetaldehyde reductase;
DE EC=1.1.1.190 {ECO:0000269|PubMed:16813561};
DE EC=1.1.1.191 {ECO:0000269|PubMed:16813561};
DE AltName: Full=AKR3C2;
GN ORFNames=SPAC19G12.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ASP-202, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16813561; DOI=10.1042/bj20060660;
RA Di Luccio E., Elling R.A., Wilson D.K.;
RT "Identification of a novel NADH-specific aldo-keto reductase using sequence
RT and structural homologies.";
RL Biochem. J. 400:105-114(2006).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=indole-3-ethanol + NAD(+) = H(+) + indole-3-acetaldehyde +
CC NADH; Xref=Rhea:RHEA:14873, ChEBI:CHEBI:15378, ChEBI:CHEBI:17890,
CC ChEBI:CHEBI:18086, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.190; Evidence={ECO:0000269|PubMed:16813561};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=indole-3-ethanol + NADP(+) = H(+) + indole-3-acetaldehyde +
CC NADPH; Xref=Rhea:RHEA:17037, ChEBI:CHEBI:15378, ChEBI:CHEBI:17890,
CC ChEBI:CHEBI:18086, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.191; Evidence={ECO:0000269|PubMed:16813561};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for NADP {ECO:0000269|PubMed:16813561};
CC KM=53.3 uM for NAD {ECO:0000269|PubMed:16813561};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16813561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB10120.1; -; Genomic_DNA.
DR PIR; T37996; T37996.
DR RefSeq; NP_594424.1; NM_001019853.2.
DR AlphaFoldDB; O13848; -.
DR SMR; O13848; -.
DR BioGRID; 278943; 1.
DR STRING; 4896.SPAC19G12.09.1; -.
DR iPTMnet; O13848; -.
DR MaxQB; O13848; -.
DR PaxDb; O13848; -.
DR PRIDE; O13848; -.
DR EnsemblFungi; SPAC19G12.09.1; SPAC19G12.09.1:pep; SPAC19G12.09.
DR GeneID; 2542483; -.
DR KEGG; spo:SPAC19G12.09; -.
DR PomBase; SPAC19G12.09; -.
DR VEuPathDB; FungiDB:SPAC19G12.09; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_3_1; -.
DR InParanoid; O13848; -.
DR OMA; DMMINPQ; -.
DR PhylomeDB; O13848; -.
DR Reactome; R-SPO-193144; Estrogen biosynthesis.
DR Reactome; R-SPO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-SPO-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR Reactome; R-SPO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-SPO-196108; Pregnenolone biosynthesis.
DR Reactome; R-SPO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-SPO-5365859; RA biosynthesis pathway.
DR Reactome; R-SPO-5652227; Fructose biosynthesis.
DR SABIO-RK; O13848; -.
DR PRO; PR:O13848; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0051268; F:alpha-keto amide reductase activity; ISO:PomBase.
DR GO; GO:0051269; F:alpha-keto ester reductase activity; ISO:PomBase.
DR GO; GO:0047018; F:indole-3-acetaldehyde reductase (NADH) activity; IDA:PomBase.
DR GO; GO:0047019; F:indole-3-acetaldehyde reductase (NADPH) activity; IDA:PomBase.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IDA:PomBase.
DR CDD; cd19120; AKR_AKR3C2-3; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044494; AKR3C2/3.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..284
FT /note="NAD/NADP-dependent indole-3-acetaldehyde reductase"
FT /id="PRO_0000339120"
FT MUTAGEN 202
FT /note="D->S: 2-fold increase of activity with NADH; no
FT activity with NADPH."
FT /evidence="ECO:0000269|PubMed:16813561"
SQ SEQUENCE 284 AA; 31570 MW; 4B33F1EC1BF14BB8 CRC64;
MLIAAMGPKI PVPAYGVGTA LFKKEKGEIN RTIVDSVKNA LAAGFIHIDC AEVYGNEEEV
GVALKEANVP RSKLFITSKV MHNVDNIPEA LNESLRKLGT DYLDLYLLHS PIPFYEKKIP
ISEGWKAMET ALGTGLVHSV GVSNFRIPDL EELLKTSTIT PRVNQIEFHP QVYKAAKPLV
EFCQSKGIIV EGYGPLSPLV RDAQGPVAEF TKSLESKYHV SDTQILLKWA YSKGVIPITT
TSKIERMKEC LNFDSFTLDK ADIDELGTLG VQHHKRTFMK HMDE
