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Protein

NADPH-dependent conjugated polyketone reductase C2

Gene

cpr-c2

Organism
Candida parapsilosis (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH.2 Publications

Enzyme regulationi

Inhibited by quercetin.1 Publication

Kineticsi

  1. KM=333 µM for ketopantoyl lactone2 Publications
  2. KM=14 µM for isatin2 Publications
  1. Vmax=481 µmol/min/mg enzyme with ketopantoyl lactone as substrate2 Publications
  2. Vmax=306 µmol/min/mg enzyme with isatin as substrate2 Publications

pH dependencei

Optimum pH is 7.2 Publications

Temperature dependencei

Optimum temperature is 40 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Proton donorBy similarity
Sitei88 – 881Lowers pKa of active site TyrBy similarity
Binding sitei125 – 1251SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 27157NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • 2-dehydropantolactone reductase (A-specific) activity Source: UniProtKB
  • aldo-keto reductase (NADP) activity Source: CGD

GO - Biological processi

  • cellular ketone metabolic process Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.214. 1133.
1.1.1.358. 1133.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH-dependent conjugated polyketone reductase C2
Short name:
CPR
Alternative name(s):
2-dehydropantolactone reductase (EC:1.1.1.358)
2-dehydropantolactone reductase (A-specific) (EC:1.1.1.168)
Ketopantoyl-lactone reductase
Gene namesi
Name:cpr-c2
OrganismiCandida parapsilosis (Yeast)
Taxonomic identifieri5480 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Organism-specific databases

CGDiCAL0000156263. CPR-C2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307NADPH-dependent conjugated polyketone reductase C2PRO_0000418423Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1
307
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Helixi27 – 293Combined sources
Beta strandi33 – 353Combined sources
Helixi40 – 5213Combined sources
Beta strandi56 – 583Combined sources
Helixi61 – 633Combined sources
Helixi66 – 7510Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 896Combined sources
Beta strandi100 – 1023Combined sources
Helixi103 – 11412Combined sources
Beta strandi119 – 1257Combined sources
Helixi131 – 1344Combined sources
Helixi139 – 15113Combined sources
Beta strandi154 – 1629Combined sources
Helixi165 – 17410Combined sources
Helixi178 – 1803Combined sources
Beta strandi184 – 1885Combined sources
Helixi200 – 2067Combined sources
Beta strandi210 – 2156Combined sources
Helixi218 – 2214Combined sources
Helixi227 – 23913Combined sources
Helixi243 – 25311Combined sources
Beta strandi257 – 2604Combined sources
Helixi265 – 2728Combined sources
Helixi281 – 29313Combined sources
Helixi301 – 3044Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VXGX-ray1.70A1-307[»]
4H8NX-ray1.80A/B1-307[»]
ProteinModelPortaliQ76L36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

KOiK19654.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q76L36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQSNLLPKT FRTKSGKEIS IALGTGTKWK QAQTINDVST ELVDNILLGL
60 70 80 90 100
KLGFRHIDTA EAYNTQKEVG EALKRTDVPR EDIWVTTKYS PGWGSIKAYS
110 120 130 140 150
KSPSDSIDKA LAQLGVDYVD LFLIHSPFFT TEQTHGYTLE QAWEALVEAK
160 170 180 190 200
KAGKVREIGI SNAAIPHLEK LFAASPSPEY YPVVNQIEFH PFLQNQSKNI
210 220 230 240 250
VRFCQEHGIL VEAFSPLAPL ARVETNALAE TLKRLAEKYK KTEAQVLLRY
260 270 280 290 300
TLQRGILPVT TSSKESRLKE SLNLFDFELT DEEVNEINKI GDANPYRAFF

HEQFKDL
Length:307
Mass (Da):34,650
Last modified:July 5, 2004 - v1
Checksum:i61BF1C153A26E953
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB084516 Genomic DNA. Translation: BAD01653.1.
JX512918 Genomic DNA. Translation: AFQ61054.1.

Genome annotation databases

KEGGiag:BAD01653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB084516 Genomic DNA. Translation: BAD01653.1.
JX512918 Genomic DNA. Translation: AFQ61054.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VXGX-ray1.70A1-307[»]
4H8NX-ray1.80A/B1-307[»]
ProteinModelPortaliQ76L36.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAD01653.

Organism-specific databases

CGDiCAL0000156263. CPR-C2.

Phylogenomic databases

KOiK19654.

Enzyme and pathway databases

BRENDAi1.1.1.214. 1133.
1.1.1.358. 1133.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCPRC2_CANPA
AccessioniPrimary (citable) accession number: Q76L36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.