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NADPH-dependent conjugated polyketone reductase C1 (CPR) (2-dehydropantolactone reductase (A-specific)) (EC 1.1.1.168) (Ketopantoyl-lactone reductase)

 CPRC1_CANPA             Reviewed;         304 AA.
Q76L37;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
15-FEB-2017, entry version 51.
RecName: Full=NADPH-dependent conjugated polyketone reductase C1;
Short=CPR;
AltName: Full=2-dehydropantolactone reductase (A-specific);
EC=1.1.1.168;
AltName: Full=Ketopantoyl-lactone reductase;
Name=cpr-c1;
Candida parapsilosis (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=5480;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 7330 / CBS 6318 / NBRC 0708 / NRRL Y-1763;
PubMed=14593510; DOI=10.1007/s00253-003-1484-3;
Kataoka M., Delacruz-Hidalgo A.R., Akond M.A., Sakuradani E., Kita K.,
Shimizu S.;
"Gene cloning and overexpression of two conjugated polyketone
reductases, novel aldo-keto reductase family enzymes, of Candida
parapsilosis.";
Appl. Microbiol. Biotechnol. 64:359-366(2004).
[2]
PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBUNIT.
STRAIN=ATCC 7330 / CBS 6318 / NBRC 0708 / NRRL Y-1763;
PubMed=11826979; DOI=10.1271/bbb.65.2785;
Hidalgo A.R., Akond M.A., Kita K., Kataoka M., Shimizu S.;
"Isolation and primary structural analysis of two conjugated
polyketone reductases from Candida parapsilosis.";
Biosci. Biotechnol. Biochem. 65:2785-2788(2001).
-!- FUNCTION: NADPH-dependent conjugated polyketone reductase with
broad substrate specificity and strict stereospecificity. Reduces
ketopantoyl lactone and isatin. Does not act on menadione, p-
nitrobenzaldehyde and pyridine-3-aldehyde.
{ECO:0000269|PubMed:11826979, ECO:0000269|PubMed:14593510}.
-!- CATALYTIC ACTIVITY: (R)-pantolactone + NADP(+) = 2-
dehydropantolactone + NADPH. {ECO:0000269|PubMed:11826979}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:11826979};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:11826979};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11826979}.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
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EMBL; AB084515; BAD01652.1; -; Genomic_DNA.
PDB; 3WG6; X-ray; 2.20 A; A/B/C/D=1-304.
PDBsum; 3WG6; -.
ProteinModelPortal; Q76L37; -.
SMR; Q76L37; -.
CGD; CAL0000154221; CPR-C1.
BRENDA; 1.1.1.214; 1133.
BRENDA; 1.1.1.358; 1133.
GO; GO:0047011; F:2-dehydropantolactone reductase (A-specific) activity; IDA:UniProtKB.
GO; GO:0042180; P:cellular ketone metabolic process; IDA:CGD.
CDD; cd06660; Aldo_ket_red; 1.
Gene3D; 3.20.20.100; -; 1.
InterPro; IPR018170; Aldo/ket_reductase_CS.
InterPro; IPR020471; Aldo/keto_reductase.
InterPro; IPR023210; NADP_OxRdtase_dom.
PANTHER; PTHR11732; PTHR11732; 1.
Pfam; PF00248; Aldo_ket_red; 1.
PIRSF; PIRSF000097; AKR; 1.
PRINTS; PR00069; ALDKETRDTASE.
SUPFAM; SSF51430; SSF51430; 1.
PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
CHAIN 1 304 NADPH-dependent conjugated polyketone
reductase C1.
/FTId=PRO_0000418422.
NP_BIND 212 268 NADP. {ECO:0000250}.
ACT_SITE 60 60 Proton donor. {ECO:0000250}.
BINDING 125 125 Substrate. {ECO:0000250}.
SITE 85 85 Lowers pKa of active site Tyr.
{ECO:0000250}.
STRAND 7 9 {ECO:0000244|PDB:3WG6}.
STRAND 15 22 {ECO:0000244|PDB:3WG6}.
HELIX 25 27 {ECO:0000244|PDB:3WG6}.
HELIX 37 49 {ECO:0000244|PDB:3WG6}.
STRAND 53 55 {ECO:0000244|PDB:3WG6}.
HELIX 58 60 {ECO:0000244|PDB:3WG6}.
HELIX 63 73 {ECO:0000244|PDB:3WG6}.
HELIX 77 79 {ECO:0000244|PDB:3WG6}.
STRAND 81 86 {ECO:0000244|PDB:3WG6}.
STRAND 99 102 {ECO:0000244|PDB:3WG6}.
HELIX 103 114 {ECO:0000244|PDB:3WG6}.
STRAND 119 124 {ECO:0000244|PDB:3WG6}.
HELIX 131 134 {ECO:0000244|PDB:3WG6}.
HELIX 138 151 {ECO:0000244|PDB:3WG6}.
STRAND 153 161 {ECO:0000244|PDB:3WG6}.
HELIX 164 172 {ECO:0000244|PDB:3WG6}.
STRAND 180 185 {ECO:0000244|PDB:3WG6}.
HELIX 197 203 {ECO:0000244|PDB:3WG6}.
STRAND 207 212 {ECO:0000244|PDB:3WG6}.
HELIX 215 218 {ECO:0000244|PDB:3WG6}.
HELIX 225 236 {ECO:0000244|PDB:3WG6}.
HELIX 240 250 {ECO:0000244|PDB:3WG6}.
STRAND 254 257 {ECO:0000244|PDB:3WG6}.
HELIX 262 269 {ECO:0000244|PDB:3WG6}.
HELIX 270 273 {ECO:0000244|PDB:3WG6}.
HELIX 278 288 {ECO:0000244|PDB:3WG6}.
HELIX 298 303 {ECO:0000244|PDB:3WG6}.
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


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