Protein Domain : IPR001128

Type:  Family Name:  Cytochrome P450
Description:  Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reaction chemistry. In mammals, these proteins are found primarily in microsomes of hepatocytes and other cell types, where they oxidise steroids, fatty acids and xenobiotics, and are important for the detoxification and clearance of various compounds, as well as for hormone synthesis and breakdown, cholesterol synthesis and vitamin D metabolism. In plants, these proteins are important for the biosynthesis of several compounds such as hormones, defensive compounds and fatty acids. In bacteria, they are important for several metabolic processes, such as the biosynthesis of antibiotic erythromycin in Saccharopolyspora erythraea(Streptomyces erythraeus).Cytochrome P450 enzymes use haem to oxidise their substrates, using protons derived from NADH or NADPH to split the oxygen so a single atom can be added to a substrate. They also require electrons, which they receive from a variety of redox partners. In certain cases, cytochrome P450 can be fused to its redox partner to produce a bi-functional protein, such as with P450BM-3 from Bacillus megaterium[], which has haem and flavin domains.Organisms produce many different cytochrome P450 enzymes (at least 58 in humans), which together with alternative splicing can provide a wide array of enzymes with different substrate and tissue specificities. Individual cytochrome P450 proteins follow the nomenclature: CYP, followed by a number (family), then a letter (subfamily), and another number (protein); e.g. CYP3A4 is the fourth protein in family 3, subfamily A. In general, family members should share >40% identity, while subfamily members should share >55% identity.Cytochrome P450 proteins can also be grouped by two different schemes. One scheme was based on a taxonomic split: class I (prokaryotic/mitochondrial) and class II (eukaryotic microsomes). The other scheme was based on the number of components in the system: class B (3-components) and class E (2-components). These classes merge to a certain degree. Most prokaryotes and mitochondria (and fungal CYP55) have 3-component systems (class I/class B) - a FAD-containing flavoprotein (NAD(P)H-dependent reductase), an iron-sulphur protein and P450. Most eukaryotic microsomes have 2-component systems (class II/class E) - NADPH:P450 reductase (FAD and FMN-containing flavoprotein) and P450. There are exceptions to this scheme, such as 1-component systems that resemble class E enzymes [, , ]. The class E enzymes can be further subdivided into five sequence clusters, groups I-V, each of which may contain more than one cytochrome P450 family (eg, CYP1 and CYP2 are both found in group I). The divergence of the cytochrome P450 superfamily into B- and E-classes, and further divergence into stable clusters within the E-class, appears to be very ancient, occurring before the appearance of eukaryotes. Short Name:  Cyt_P450

6 Child Features

DB identifier Type Name
IPR002403 Family Cytochrome P450, E-class, group IV
IPR002401 Family Cytochrome P450, E-class, group I
IPR002397 Family Cytochrome P450, B-class
IPR002402 Family Cytochrome P450, E-class, group II
IPR002399 Family Cytochrome P450, mitochondrial
IPR002949 Family Cytochrome P450, E-class, CYP24A, mitochondrial

1 Contains

DB identifier Type Name
IPR017972 Conserved_site Cytochrome P450, conserved site

4 Cross Referencess

Identifier
SSF48264
PF00067
PR00385
G3DSA:1.10.630.10

0 Found In

4 GO Annotations

GO Term Gene Name Organism
GO:0005506 IPR001128
GO:0016705 IPR001128
GO:0020037 IPR001128
GO:0055114 IPR001128

0 Parent Features

36122 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
107475 D8S2S0 PAC:15420826 Selaginella moellendorffii 419  
135524 D8TAG1 PAC:15414960 Selaginella moellendorffii 79  
425677 D8STX6 PAC:15406728 Selaginella moellendorffii 131  
103517 D8RWT8 PAC:15409727 Selaginella moellendorffii 480  
104195 D8RY45 PAC:15409801 Selaginella moellendorffii 509  
113134 B2XCI8 PAC:15414051 Selaginella moellendorffii 508  
113458 D8SC30 PAC:15416294 Selaginella moellendorffii 463  
116233 D8SG92 PAC:15423366 Selaginella moellendorffii 333  
116580 D8SGT9 PAC:15403456 Selaginella moellendorffii 479  
117920 D8SIN6 PAC:15409403 Selaginella moellendorffii 492  
118120 D8SIP5 PAC:15406147 Selaginella moellendorffii 487  
119072 D8SJW3 PAC:15408417 Selaginella moellendorffii 518  
12223 D8SCL8 PAC:15403766 Selaginella moellendorffii 464  
12227 D8SCL6 PAC:15403771 Selaginella moellendorffii 464  
12239 D8RJU8 PAC:15403795 Selaginella moellendorffii 464  
12447 D8R5W8 PAC:15405418 Selaginella moellendorffii 477  
128662 D8SZS1 PAC:15417321 Selaginella moellendorffii 497  
406844 D8R346 PAC:15419141 Selaginella moellendorffii 424  
145597 D8RBG8 PAC:15422129 Selaginella moellendorffii 563  
15275 D8T0A5 PAC:15412803 Selaginella moellendorffii 228  
158927 D8SWE9 PAC:15418809 Selaginella moellendorffii 503  
159100 D8SX72 PAC:15415603 Selaginella moellendorffii 444  
165663 D8QVV0 PAC:15415068 Selaginella moellendorffii 424  
171715 D8RIA8 PAC:15411229 Selaginella moellendorffii 511  
172829 D8RMX3 PAC:15414952 Selaginella moellendorffii 508  
18538 D8SSP4 PAC:15401403 Selaginella moellendorffii 111  
20611 D8QQT8 PAC:15408196 Selaginella moellendorffii 430  
230371 PAC:15413206 Selaginella moellendorffii 793  
235879 D8T2K0 PAC:15409280 Selaginella moellendorffii 488  
271334 D8S625 PAC:15422353 Selaginella moellendorffii 485  

4 Publications

First Author Title Year Journal Volume Pages PubMed ID
            16042601
            17023115
            15128046
            8637843