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Conserved domains on  [gi|2462581021|ref|XP_054179732|]
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prostacyclin synthase isoform X1 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

cytochrome P450 family protein may catalyze the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 52-225 1.83e-103

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


The actual alignment was detected with superfamily member cd20634:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 442  Bit Score: 307.07  E-value: 1.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021  52 SFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHR 131
Cdd:cd20634     1 KFLTRMKEKHGDIFTVQVAGRYVTVLLDPHSYDAVVWEPSTSLDFTSYARLLMDRIFDVQLPSYDPTEEKKRMESHFQGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021 132 ELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLD 211
Cdd:cd20634    81 NLTQLTQAMFNNLQLLLLGDAMGLSTEWKKDGLFNFCYSLLFRAGYLTLFGNENENSTHESQNKDRAHSAEVYHEFRKLD 160

                         170
                  ....*....|....
gi 2462581021 212 RLLPKLARGSLSVG 225
Cdd:cd20634   161 QLLPKLARGTLSKE 174
 
Name Accession Description Interval E-value
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 52-225 1.83e-103

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 307.07  E-value: 1.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021  52 SFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHR 131
Cdd:cd20634     1 KFLTRMKEKHGDIFTVQVAGRYVTVLLDPHSYDAVVWEPSTSLDFTSYARLLMDRIFDVQLPSYDPTEEKKRMESHFQGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021 132 ELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLD 211
Cdd:cd20634    81 NLTQLTQAMFNNLQLLLLGDAMGLSTEWKKDGLFNFCYSLLFRAGYLTLFGNENENSTHESQNKDRAHSAEVYHEFRKLD 160

                         170
                  ....*....|....
gi 2462581021 212 RLLPKLARGSLSVG 225
Cdd:cd20634   161 QLLPKLARGTLSKE 174
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 27-80 1.43e-04

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 42.65  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462581021  27 PGEPPLdlgsiPWLGYALDFGKDA--ASFLTRMKEKHGDIFTILVGGRYVTVLLDP 80
Cdd:pfam00067   2 PGPPPL-----PLFGNLLQLGRKGnlHSVFTKLQKKYGPIFRLYLGPKPVVVLSGP 52
 
Name Accession Description Interval E-value
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 52-225 1.83e-103

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 307.07  E-value: 1.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021  52 SFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHR 131
Cdd:cd20634     1 KFLTRMKEKHGDIFTVQVAGRYVTVLLDPHSYDAVVWEPSTSLDFTSYARLLMDRIFDVQLPSYDPTEEKKRMESHFQGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021 132 ELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLD 211
Cdd:cd20634    81 NLTQLTQAMFNNLQLLLLGDAMGLSTEWKKDGLFNFCYSLLFRAGYLTLFGNENENSTHESQNKDRAHSAEVYHEFRKLD 160

                         170
                  ....*....|....
gi 2462581021 212 RLLPKLARGSLSVG 225
Cdd:cd20634   161 QLLPKLARGTLSKE 174
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 54-223 9.63e-42

cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also called 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) or sterol 12-alpha-hydroxylase. It is involved in the classic (or neutral) pathway of cholesterol catabolism and bile acid synthesis, and is responsible for sterol 12alpha-hydroxylation, which directs the synthesis to cholic acid (CA). It converts 7-alpha-hydroxy-4-cholesten-3-one into 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one, but also displays broad substrate specificity including other 7-alpha-hydroxylated C27 steroids. CYP8B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 147.90  E-value: 9.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021  54 LTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQlphySPSDEKARMKLT----LL 129
Cdd:cd20633     1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKESKSKLDFGKFASELVLRVFGYQ----PTENDHKMLQTLstkhLM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021 130 HRELQALTEAMYTNLHAVLL-GDATEAGSG-WHEMGLLDFSYSFLLRAGYLTLYGIE---ALPRTHESQAQDRVHSADVF 204
Cdd:cd20633    77 GDGLVVLNQAMMENLQNLMLhSKGSGDGGReWQQDGLFHYSYNIVFRAGYLALFGNEpdkEAGNKEKAKEQDLLHSEELF 156

                         170
                  ....*....|....*....
gi 2462581021 205 HTFRQLDRLLPKLARGSLS 223
Cdd:cd20633   157 EEFRKFDQLFPRLAYSVLP 175
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 53-220 2.37e-23

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 97.83  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021  53 FLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTrLDFHAYAIFLMERIFDVQlpHYSPSDEKARMKL------ 126
Cdd:cd20631     1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYHSVIRHGKH-LDWKKFHFATSAKAFGHV--SFDPSDGNTTENIhdtfik 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021 127 TLLHRELQALTEAMYTNLHAVLLGDAT--EAGSGWHEMGLLDFSYSFLLRAGYLTLYG--IEALPRTHESQAQDRVHSAD 202
Cdd:cd20631    78 TLQGSALDSLTESMMENLQYVMLQDKSssSSTKAWVTEGLYSFCYRVMFEAGYLTLFGkeLTAREDKNARLEAQRALILN 157

                         170
                  ....*....|....*...
gi 2462581021 203 VFHTFRQLDRLLPKLARG 220
Cdd:cd20631   158 ALENFKEFDKVFPALVAG 175
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 53-218 5.08e-21

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410725  Cd Length: 438  Bit Score: 91.21  E-value: 5.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021  53 FLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVwEPRTRLDFHAYAIFLMERIFD---VQLPHYSPSDEKARMKLTLL 129
Cdd:cd20632     1 FLLALQKKHGDVFTVLIAGKYITFIMDPFLYPYVI-KHGKQLDFHEFSDRLASKTFGyppLRSPKFPGLNEQIHRSYQYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581021 130 H-RELQALTEAMYTNLHAVLLGDATEAGSGWHEmGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVhsadvfhTFR 208
Cdd:cd20632    80 QgENLDILTESMMGNLQLVLRQQFLGETDWETE-ELYEFCSRIMFEATFLTLYGKPPDDDRHKVISELRK-------KFR 151

                         170
                  ....*....|
gi 2462581021 209 QLDRLLPKLA 218
Cdd:cd20632   152 KFDAMFPYLV 161
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 27-80 1.43e-04

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 42.65  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462581021  27 PGEPPLdlgsiPWLGYALDFGKDA--ASFLTRMKEKHGDIFTILVGGRYVTVLLDP 80
Cdd:pfam00067   2 PGPPPL-----PLFGNLLQLGRKGnlHSVFTKLQKKYGPIFRLYLGPKPVVVLSGP 52
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 53-96 7.33e-03

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 37.29  E-value: 7.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462581021  53 FLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPrtRLDF 96
Cdd:cd20635     4 FIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSK--DVDF 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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