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Protein

Prostaglandin F synthase

Gene

P100/11E

Organism
Leishmania major
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + 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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Keywords - Ligandi

NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin F synthase (EC:1.1.1.188)
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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001246531 – 284Prostaglandin F synthaseAdd 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.
OMAiVELHPLN.

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.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

STRINGi5664.LmjF.31.2150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
HOGENOMiHOG000250272.
InParanoidiP22045.
OMAiVELHPLN.

Enzyme and pathway databases

UniPathwayiUPA00662.

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.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGFS_LEIMA
AccessioniPrimary (citable) accession number: P22045
Secondary accession number(s): Q4Q646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 3, 2012
Last modified: November 2, 2016
This is version 79 of the entry and version 3 of the sequence. [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

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.