| General Information |
| MoonProt ID | 131 |
| First appeared in release | 1.0 |
| Name(s) | Prostaglandin H2 Synthase
Prostaglandin G/H synthase 1
Cyclooxygenase-1
Prostaglandin-endoperoxide synthase 1
COX-1
COX1
Prostaglandin H2 synthase 1
PGH synthase 1
PGHS-1
PHS 1
Prostaglandin-endoperoxide synthase 1
Gene Name: PTGS1
|
| UniProt ID | P05979 (PGH1_SHEEP) Reviewed |
| GO terms | GO:0001516 prostaglandin biosynthetic process
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006693 prostaglandin metabolic process
GO:0006979 response to oxidative stress
GO:0008217 regulation of blood pressure
GO:0055114 oxidation-reduction process
GO:0004601 peroxidase activity
GO:0004666 prostaglandin-endoperoxide synthase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0031090 organelle membrane
GO:0043231 intracellular membrane-bounded organelle |
| Organisms for which functions have been demonstrated | Ovis aries (Sheep) |
| Sequence length | 600 |
| FASTA sequence | >sp|P05979|PGH1_SHEEP Prostaglandin G/H synthase 1 OS=Ovis aries GN=PTGS1 PE=1 SV=3
MSRQSISLRFPLLLLLLSPSPVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFMLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPRQEDRPGVERPPTEL" |
| Structure Information |
| PDB ID | 1HT8,
2OYU,
1CQE,
1EQG,
1EQH,
1PGF,
1PGG,
1FE2,
1IGZ,
1IGX,
1PGE,
1PTH,
1Q4G,
2AYL,
3KK6, 3N8V, 3N8W, 3N8X, 3N8Y, 3N8Z, 2OYE, 1PRH, 1HT5, 1U67, 1PTH, 1DIY, 3N8Y, 3N8W, 1PRH, 1HT5, 1EBV |
| Quaternary structure | |
| SCOP | Heme-dependent peroxidases, Knottins (small inhibitors, toxins, lectins) |
| CATH | 2.10.25.10, 1.10.640.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-7, 131-143, 415-417 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Prostaglandin H2 synthase-1, enzyme
Arachidonate + AH(2) + 2 O(2) <=> prostaglandin H(2) + A + H(2)O
Lipid metabolism, prostaglandin biosynthesis |
| References for function | Picot D, Loll PJ, Garavito RM. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature. 1994 Jan 20. PMID: 8121489 |
| E.C. number | 1.14.99.1 |
| Location of functional site(s) | |
| Cellular location of function | Endoplasmic Reticulum membrane, transmembrane protein |
| Comments | |
| Function 2 |
| Function description | Peroxidase and cyclo-oxygenase 2 phenolic donor + H(2)O(2) <=> 2 phenoxyl radical of the donor + 2 H(2)O |
| References for function | Selinsky BS, Gupta K, Sharkey CT, Loll PJ. Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Biochemistry. 2001 May 1. PMID: 11318639 |
| E.C. number | 1.11.1.7 |
| Location of functional site(s) | |
| Cellular location of function | Cytoplasm |
| Comments | Active site containing Tyr385, Tyr355, Ser530, Glu524, Arg120 interactions. Synthesis and use of iodinated nonsteroidal antiinflammatory drug analogs as crystallographic probes of the prostaglandin H2 synthase cyclooxygenase active site. Loll PJ, Picot D, Ekabo O, Garavito RM. Biochemistry. 1996 Jun 11;35(23):7330-40. PMID: 8652509
Active site containg Arg277, Gln358, Arg120, Ile -523, Tyr355 play roles in the inhibition activity.
Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Selinsky BS, Gupta K, Sharkey CT, Loll PJ. Biochemistry. 2001 May 1;40(17):5172-80. PMID: 11318639 |