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Protein

9,11-endoperoxide prostaglandin H2 reductase

Gene

P100/11E

Organism
Leishmania major
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. Has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.1 Publication

Catalytic activityi

Prostaglandin F2alpha + NADP+ = prostaglandin H2 + NADPH.1 Publication

Kineticsi

  1. KM=15 µM for prostaglandin H21 Publication
  2. KM=12.5 µM for 9,10-phenanthrenequinone1 Publication
  3. KM=12.8 µM for p-nitrobenzaldehyde1 Publication
  4. KM=3 µM for NADPH1 Publication
  1. Vmax=270 nmol/min/mg enzyme toward prostaglandin H21 Publication
  2. Vmax=4780 nmol/min/mg enzyme toward 9,10-phenanthrenequinone1 Publication
  3. Vmax=7280 nmol/min/mg enzyme toward p-nitrobenzaldehyde1 Publication

Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei49NADPBy similarity1
Active sitei54Proton donorBy similarity1
Sitei79Lowers pKa of active site TyrBy similarity1
Binding sitei112SubstrateBy similarity1
Binding sitei171NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi24 – 25NADPBy similarity2
Nucleotide bindingi149 – 150NADPBy similarity2
Nucleotide bindingi197 – 202NADPBy similarity6
Nucleotide bindingi240 – 242NADPBy similarity3
Nucleotide bindingi246 – 250NADPBy similarity5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism
LigandNADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00662

Names & Taxonomyi

Protein namesi
Recommended name:
9,11-endoperoxide prostaglandin H2 reductase1 Publication (EC:1.1.1.-1 Publication)
Alternative name(s):
Prostaglandin F2-alpha synthase
Gene namesi
Name:P100/11E
OrganismiLeishmania major
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 31

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001246531 – 2849,11-endoperoxide prostaglandin H2 reductaseAdd BLAST284

Expressioni

Developmental stagei

P110/11E abundance is markedly elevated in promastigotes relative to amastigotes.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi5664.LmjF.31.2150

Structurei

Secondary structure

1284
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Beta strandi8 – 10Combined sources3
Beta strandi16 – 20Combined sources5
Helixi31 – 42Combined sources12
Beta strandi47 – 49Combined sources3
Helixi52 – 54Combined sources3
Helixi57 – 67Combined sources11
Helixi71 – 73Combined sources3
Beta strandi75 – 80Combined sources6
Helixi82 – 84Combined sources3
Helixi87 – 101Combined sources15
Beta strandi106 – 111Combined sources6
Helixi117 – 123Combined sources7
Helixi126 – 139Combined sources14
Beta strandi142 – 150Combined sources9
Helixi153 – 160Combined sources8
Beta strandi169 – 173Combined sources5
Helixi181 – 189Combined sources9
Beta strandi193 – 198Combined sources6
Helixi201 – 203Combined sources3
Helixi205 – 207Combined sources3
Helixi209 – 217Combined sources9
Helixi222 – 232Combined sources11
Helixi244 – 251Combined sources8
Helixi260 – 267Combined sources8
Turni279 – 281Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F40X-ray1.60A/B1-284[»]
4G5DX-ray1.80A/B1-284[»]
ProteinModelPortaliP22045
SMRiP22045
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577 Eukaryota
COG0656 LUCA
HOGENOMiHOG000250272
InParanoidiP22045
OMAiTHGYEST

Family and domain databases

CDDicd06660 Aldo_ket_red, 1 hit
Gene3Di3.20.20.100, 1 hit
InterProiView protein in InterPro
IPR018170 Aldo/ket_reductase_CS
IPR020471 Aldo/keto_reductase
IPR023210 NADP_OxRdtase_dom
IPR036812 NADP_OxRdtase_dom_sf
PfamiView protein in Pfam
PF00248 Aldo_ket_red, 1 hit
PIRSFiPIRSF000097 AKR, 1 hit
PRINTSiPR00069 ALDKETRDTASE
SUPFAMiSSF51430 SSF51430, 1 hit
PROSITEiView protein in PROSITE
PS00798 ALDOKETO_REDUCTASE_1, 1 hit
PS00062 ALDOKETO_REDUCTASE_2, 1 hit
PS00063 ALDOKETO_REDUCTASE_3, 1 hit

Sequencei

Sequence statusi: Complete.

P22045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVDKAMVT LSNGVKMPQF GLGVWQSPAG EVTENAVKWA LCAGYRHIDT
60 70 80 90 100
AAIYKNEESV GAGLRASGVP REDVFITTKL WNTEQGYEST LAAFEESRQK
110 120 130 140 150
LGVDYIDLYL IHWPRGKDIL SKEGKKYLDS WRAFEQLYKE KKVRAIGVSN
160 170 180 190 200
FHIHHLEDVL AMCTVTPMVN QVELHPLNNQ ADLRAFCDAK QIKVEAWSPL
210 220 230 240 250
GQGKLLSNPI LSAIGAKYNK TAAQVILRWN IQKNLITIPK SVHRERIEEN
260 270 280
ADIFDFELGA EDVMSIDALN TNSRYGPDPD EAQF
Length:284
Mass (Da):31,850
Last modified:October 3, 2012 - v3
Checksum:iD2FF5967F7EDC767
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38K → N in AAA57350 (PubMed:2918000).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04483 mRNA Translation: AAA57350.1
FR796427 Genomic DNA Translation: CAJ08404.1
PIRiA32950
RefSeqiXP_001685202.1, XM_001685150.1

Genome annotation databases

EnsemblProtistsiLmjF.31.2150:mRNA; LmjF.31.2150:pep; LmjF.31.2150
GeneIDi5654147
KEGGilma:LMJF_31_2150

Similar proteinsi

Entry informationi

Entry nameiPGFS_LEIMA
AccessioniPrimary (citable) accession number: P22045
Secondary accession number(s): Q4Q646
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 3, 2012
Last modified: April 25, 2018
This is version 84 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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