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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491NADPBy similarity
Active sitei54 – 541Proton donorBy similarity
Sitei79 – 791Lowers pKa of active site TyrBy similarity
Binding sitei112 – 1121SubstrateBy similarity
Binding sitei171 – 1711NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 252NADPBy similarity
Nucleotide bindingi149 – 1502NADPBy similarity
Nucleotide bindingi197 – 2026NADPBy similarity
Nucleotide bindingi240 – 2423NADPBy similarity
Nucleotide bindingi246 – 2505NADPBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Prostaglandin F synthasePRO_0000124653Add
BLAST

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

1
284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Beta strandi8 – 103Combined sources
Beta strandi16 – 205Combined sources
Helixi31 – 4212Combined sources
Beta strandi47 – 493Combined sources
Helixi52 – 543Combined sources
Helixi57 – 6711Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 806Combined sources
Helixi82 – 843Combined sources
Helixi87 – 10115Combined sources
Beta strandi106 – 1116Combined sources
Helixi117 – 1237Combined sources
Helixi126 – 13914Combined sources
Beta strandi142 – 1509Combined sources
Helixi153 – 1608Combined sources
Beta strandi169 – 1735Combined sources
Helixi181 – 1899Combined sources
Beta strandi193 – 1986Combined sources
Helixi201 – 2033Combined sources
Helixi205 – 2073Combined sources
Helixi209 – 2179Combined sources
Helixi222 – 23211Combined sources
Helixi244 – 2518Combined sources
Helixi260 – 2678Combined sources
Turni279 – 2813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F40X-ray1.60A/B1-284[»]
4G5DX-ray1.80A/B1-284[»]
ProteinModelPortaliP22045.
SMRiP22045. Positions 9-280.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381K → N in AAA57350 (PubMed:2918000).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4F40X-ray1.60A/B1-284[»]
4G5DX-ray1.80A/B1-284[»]
ProteinModelPortaliP22045.
SMRiP22045. Positions 9-280.
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: September 7, 2016
This is version 77 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.