CPRC2_CANPA
ID CPRC2_CANPA Reviewed; 307 AA.
AC Q76L36;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=NADPH-dependent conjugated polyketone reductase C2;
DE Short=CPR;
DE AltName: Full=2-dehydropantolactone reductase;
DE EC=1.1.1.358;
DE AltName: Full=2-dehydropantolactone reductase (A-specific);
DE EC=1.1.1.168;
DE AltName: Full=Ketopantoyl-lactone reductase;
GN Name=cpr-c2;
OS Candida parapsilosis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5480;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 7330 / CBS 6318 / NBRC 0708 / NRRL Y-1763;
RX PubMed=14593510; DOI=10.1007/s00253-003-1484-3;
RA Kataoka M., Delacruz-Hidalgo A.R., Akond M.A., Sakuradani E., Kita K.,
RA Shimizu S.;
RT "Gene cloning and overexpression of two conjugated polyketone reductases,
RT novel aldo-keto reductase family enzymes, of Candida parapsilosis.";
RL Appl. Microbiol. Biotechnol. 64:359-366(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16970545; DOI=10.1146/annurev.pharmtox.47.120505.105337;
RA Jin Y., Penning T.M.;
RT "Aldo-keto reductases and bioactivation/detoxication.";
RL Annu. Rev. Pharmacol. Toxicol. 47:263-292(2007).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 7330 / CBS 6318 / NBRC 0708 / NRRL Y-1763;
RX PubMed=11826979; DOI=10.1271/bbb.65.2785;
RA Hidalgo A.R., Akond M.A., Kita K., Kataoka M., Shimizu S.;
RT "Isolation and primary structural analysis of two conjugated polyketone
RT reductases from Candida parapsilosis.";
RL Biosci. Biotechnol. Biochem. 65:2785-2788(2001).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBUNIT.
RC STRAIN=ATCC 7330 / CBS 6318 / NBRC 0708 / NRRL Y-1763;
RX PubMed=2644973; DOI=10.1016/s0304-4165(89)80031-5;
RA Hata H., Shimizu S., Hattori S., Yamada H.;
RT "Ketopantoyl-lactone reductase from Candida parapsilosis: purification and
RT characterization as a conjugated polyketone reductase.";
RL Biochim. Biophys. Acta 990:175-181(1989).
CC -!- FUNCTION: NADPH-dependent conjugated polyketone reductase with broad
CC substrate specificity and strict stereospecificity. Reduces ketopantoyl
CC lactone and isatin. Does not act on menadione, p-nitrobenzaldehyde and
CC pyridine-3-aldehyde. {ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:14593510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantolactone + NADP(+) = 2-dehydropantolactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:18981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16719,
CC ChEBI:CHEBI:18395, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.358; Evidence={ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:2644973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantolactone + NADP(+) = 2-dehydropantolactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:18981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16719,
CC ChEBI:CHEBI:18395, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.168; Evidence={ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:2644973};
CC -!- ACTIVITY REGULATION: Inhibited by quercetin.
CC {ECO:0000269|PubMed:2644973}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=333 uM for ketopantoyl lactone {ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:2644973};
CC KM=14 uM for isatin {ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:2644973};
CC Vmax=481 umol/min/mg enzyme with ketopantoyl lactone as substrate
CC {ECO:0000269|PubMed:11826979, ECO:0000269|PubMed:2644973};
CC Vmax=306 umol/min/mg enzyme with isatin as substrate
CC {ECO:0000269|PubMed:11826979, ECO:0000269|PubMed:2644973};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:2644973};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:11826979, ECO:0000269|PubMed:2644973};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11826979,
CC ECO:0000269|PubMed:2644973}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB084516; BAD01653.1; -; Genomic_DNA.
DR EMBL; JX512918; AFQ61054.1; -; Genomic_DNA.
DR PDB; 3VXG; X-ray; 1.70 A; A=1-307.
DR PDB; 4H8N; X-ray; 1.80 A; A/B=1-307.
DR PDBsum; 3VXG; -.
DR PDBsum; 4H8N; -.
DR AlphaFoldDB; Q76L36; -.
DR SMR; Q76L36; -.
DR KEGG; ag:BAD01653; -.
DR CGD; CAL0000156263; CPR-C2.
DR VEuPathDB; FungiDB:CPAR2_703660; -.
DR BRENDA; 1.1.1.214; 1133.
DR BRENDA; 1.1.1.358; 1133.
DR GO; GO:0047011; F:2-dehydropantolactone reductase (A-specific) activity; IDA:UniProtKB.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:CGD.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:InterPro.
DR GO; GO:0042180; P:cellular ketone metabolic process; IDA:CGD.
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; IPR018170; Aldo/ket_reductase_CS.
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.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..307
FT /note="NADPH-dependent conjugated polyketone reductase C2"
FT /id="PRO_0000418423"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215..271
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 88
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4H8N"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:3VXG"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:3VXG"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:3VXG"
SQ SEQUENCE 307 AA; 34650 MW; 61BF1C153A26E953 CRC64;
MTQSNLLPKT FRTKSGKEIS IALGTGTKWK QAQTINDVST ELVDNILLGL KLGFRHIDTA
EAYNTQKEVG EALKRTDVPR EDIWVTTKYS PGWGSIKAYS KSPSDSIDKA LAQLGVDYVD
LFLIHSPFFT TEQTHGYTLE QAWEALVEAK KAGKVREIGI SNAAIPHLEK LFAASPSPEY
YPVVNQIEFH PFLQNQSKNI VRFCQEHGIL VEAFSPLAPL ARVETNALAE TLKRLAEKYK
KTEAQVLLRY TLQRGILPVT TSSKESRLKE SLNLFDFELT DEEVNEINKI GDANPYRAFF
HEQFKDL
