CPRC1_CANPA
ID CPRC1_CANPA Reviewed; 304 AA.
AC Q76L37;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=NADPH-dependent conjugated polyketone reductase C1;
DE Short=CPR;
DE AltName: Full=2-dehydropantolactone reductase (A-specific);
DE EC=1.1.1.168;
DE AltName: Full=Ketopantoyl-lactone reductase;
GN Name=cpr-c1;
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 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).
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=1.1.1.168; Evidence={ECO:0000269|PubMed:11826979};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11826979};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:11826979};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11826979}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB084515; BAD01652.1; -; Genomic_DNA.
DR PDB; 3WG6; X-ray; 2.20 A; A/B/C/D=1-304.
DR PDBsum; 3WG6; -.
DR AlphaFoldDB; Q76L37; -.
DR SMR; Q76L37; -.
DR CGD; CAL0000154221; CPR-C1.
DR VEuPathDB; FungiDB:CPAR2_109870; -.
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: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; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..304
FT /note="NADPH-dependent conjugated polyketone reductase C1"
FT /id="PRO_0000418422"
FT ACT_SITE 60
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212..268
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 85
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:3WG6"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:3WG6"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:3WG6"
SQ SEQUENCE 304 AA; 34492 MW; E13A1C04B2A1388F CRC64;
MSLAGKEFKL SNGNKIPAVA FGTGTKYFKR GHNDLDKQLI GTLELALRSG FRHIDGAEIY
GTNKEIGIAL KNVGLNRKDV FITDKYNSGN HTYDGKHSKH QNPYNALKAD LEDLGLEYVD
LYLIHFPYIS EKSHGFDLVE AWRYLERAKN EGLARNIGVS NFTIENLKSI LDANTDSIPV
VNQIEFSAYL QDQTPGIVEY SQQQGILIEA YGPLGPITQG RPGPLDKVLS KLSEKYKRNE
GQILLRWVLQ RGILPITTTS KEERINDVLE IFDFELDKED EDQITKVGKE KTLRQFSKEY
SKYD
