BZRD_YEAST
ID BZRD_YEAST Reviewed; 263 AA.
AC P40580; D6VVW7; Q54AB5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Benzil reductase ((S)-benzoin forming) IRC24;
DE EC=1.1.1.320;
DE AltName: Full=Increased recombination centers protein 24;
GN Name=IRC24; OrderedLocusNames=YIR036C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY AS BENZIL REDUCTASE,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=11796169; DOI=10.1016/s0168-1656(01)00426-6;
RA Maruyama R., Nishizawa M., Itoi Y., Ito S., Inoue M.;
RT "The enzymes with benzil reductase activity conserved from bacteria to
RT mammals.";
RL J. Biotechnol. 94:157-169(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP INDUCTION.
RX PubMed=17163986; DOI=10.1186/1471-2164-7-313;
RA Fry R.C., DeMott M.S., Cosgrove J.P., Begley T.J., Samson L.D., Dedon P.C.;
RT "The DNA-damage signature in Saccharomyces cerevisiae is associated with
RT single-strand breaks in DNA.";
RL BMC Genomics 7:313-313(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18085829; DOI=10.1371/journal.pgen.0030228;
RA Alvaro D., Lisby M., Rothstein R.;
RT "Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting
RT recombination.";
RL PLoS Genet. 3:E228-E228(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Reduces benzil stereospecifically to (S)-benzoin. Is probably
CC involved in a pathway contributing to genomic integrity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-benzoin + NADP(+) = benzil + H(+) + NADPH;
CC Xref=Rhea:RHEA:25968, ChEBI:CHEBI:15378, ChEBI:CHEBI:51507,
CC ChEBI:CHEBI:51510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.320; Evidence={ECO:0000269|PubMed:11796169};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=207 uM for benzil {ECO:0000269|PubMed:11796169};
CC KM=29 uM for 1-phenyl-1,2-propanedione {ECO:0000269|PubMed:11796169};
CC -!- INDUCTION: By single-strand DNA damage. {ECO:0000269|PubMed:17163986}.
CC -!- DISRUPTION PHENOTYPE: Displays increased levels of spontaneous RAD52
CC foci in proliferating diploid cells. {ECO:0000269|PubMed:18085829}.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; Z38061; CAA86196.1; -; Genomic_DNA.
DR EMBL; AY558240; AAS56566.1; -; Genomic_DNA.
DR EMBL; AB052924; BAB86002.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08583.1; -; Genomic_DNA.
DR PIR; S48498; S48498.
DR RefSeq; NP_012302.3; NM_001179558.3.
DR AlphaFoldDB; P40580; -.
DR SMR; P40580; -.
DR BioGRID; 35027; 30.
DR DIP; DIP-4707N; -.
DR STRING; 4932.YIR036C; -.
DR MaxQB; P40580; -.
DR PaxDb; P40580; -.
DR PRIDE; P40580; -.
DR EnsemblFungi; YIR036C_mRNA; YIR036C; YIR036C.
DR GeneID; 854854; -.
DR KEGG; sce:YIR036C; -.
DR SGD; S000001475; IRC24.
DR VEuPathDB; FungiDB:YIR036C; -.
DR eggNOG; KOG1204; Eukaryota.
DR GeneTree; ENSGT00940000176436; -.
DR HOGENOM; CLU_010194_2_11_1; -.
DR InParanoid; P40580; -.
DR OMA; RVWAVDP; -.
DR BioCyc; YEAST:G3O-31450-MON; -.
DR PRO; PR:P40580; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40580; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0102306; F:benzil reductase [(S)-benzoin-forming] activity; IEA:UniProtKB-EC.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:SGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..263
FT /note="Benzil reductase ((S)-benzoin forming) IRC24"
FT /id="PRO_0000054871"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 6..30
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 28804 MW; 53DE25425AAC946F CRC64;
MGKVILITGA SRGIGLQLVK TVIEEDDECI VYGVARTEAG LQSLQREYGA DKFVYRVLDI
TDRSRMEALV EEIRQKHGKL DGIVANAGML EPVKSISQSN SEHDIKQWER LFDVNFFSIV
SLVALCLPLL KSSPFVGNIV FVSSGASVKP YNGWSAYGCS KAALNHFAMD IASEEPSDKV
RAVCIAPGVV DTQMQKDIRE TLGPQGMTPK ALERFTQLYK TSSLLDPKVP AAVLAQLVLK
GIPDSLNGQY LRYNDERLGP VQG
