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Protein

Prostaglandin F synthase

Gene
N/A
Organism
Trypanosoma brucei brucei
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 towards 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=1.3 µM for prostaglandin H21 Publication
  2. KM=0.42 µM for 9,10-phenanthrenequinone1 Publication
  3. KM=0.8 µM for p-nitrobenzaldehyde1 Publication
  4. KM=5.7 µM for NADPH1 Publication
  1. Vmax=2 µmol/min/mg enzyme toward prostaglandin H21 Publication
  2. Vmax=22 µmol/min/mg enzyme toward p-nitrobenzaldehyde1 Publication
  3. Vmax=48 µmol/min/mg enzyme toward 9,10-phenanthrenequinone1 Publication

pH dependencei

Optimum pH is 6-9.1 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 sitei47NADP1 Publication1
Active sitei52Proton donorBy similarity1
Sitei77Lowers pKa of active site TyrBy similarity1
Binding sitei110SubstrateBy similarity1
Binding sitei161NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi22 – 23NADP1 Publication2
Nucleotide bindingi139 – 140NADP1 Publication2
Nucleotide bindingi187 – 192NADP1 Publication6
Nucleotide bindingi230 – 232NADP1 Publication3
Nucleotide bindingi236 – 240NADP1 Publication5

GO - Molecular functioni

GO - Biological processi

  • D-arabinose catabolic process Source: GeneDB
  • prostaglandin biosynthetic process Source: UniProtKB-UniPathway
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
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004194931 – 276Prostaglandin F synthaseAdd BLAST276

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi14 – 18Combined sources5
Helixi29 – 41Combined sources13
Beta strandi45 – 47Combined sources3
Helixi50 – 52Combined sources3
Helixi55 – 64Combined sources10
Beta strandi65 – 67Combined sources3
Helixi69 – 71Combined sources3
Beta strandi73 – 78Combined sources6
Helixi80 – 82Combined sources3
Helixi85 – 99Combined sources15
Beta strandi104 – 110Combined sources7
Helixi117 – 129Combined sources13
Beta strandi132 – 134Combined sources3
Beta strandi136 – 140Combined sources5
Helixi143 – 150Combined sources8
Beta strandi158 – 163Combined sources6
Helixi171 – 179Combined sources9
Beta strandi183 – 188Combined sources6
Helixi191 – 193Combined sources3
Turni194 – 197Combined sources4
Helixi199 – 206Combined sources8
Turni207 – 209Combined sources3
Helixi212 – 222Combined sources11
Helixi234 – 241Combined sources8
Helixi250 – 257Combined sources8
Turni269 – 271Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VBJX-ray2.10A/B1-276[»]
ProteinModelPortaliQ9GV41.
SMRiQ9GV41.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GV41.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

HOGENOMiHOG000250272.

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]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GV41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTQSLKLS NGVMMPVLGF GMWKLQDGNE AETATMWAIK SGYRHIDTAA
60 70 80 90 100
IYKNEESAGR AIASCGVPRE ELFVTTKLWN SDQGYESTLS AFEKSIKKLG
110 120 130 140 150
LEYVDLYLIH WPGKDKFIDT WKAFEKLYAD KKVRAIGVSN FHEHHIEELL
160 170 180 190 200
KHCKVAPMVN QIELHPLLNQ KALCEYCKSK NIAVTAWSPL GQGHLVEDAR
210 220 230 240 250
LKAIGGKYGK TAAQVMLRWE IQAGVITIPK SGNEARIKEN GNIFDFELTA
260 270
EDIQVIDGMN AGHRYGPDPE VFMNDF
Length:276
Mass (Da):30,993
Last modified:March 1, 2001 - v1
Checksum:iD57ECDCCEE8B6971
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034727 mRNA. Translation: BAB17681.1.

Genome annotation databases

GeneDBiTb927.11.4700:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034727 mRNA. Translation: BAB17681.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VBJX-ray2.10A/B1-276[»]
ProteinModelPortaliQ9GV41.
SMRiQ9GV41.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiTb927.11.4700:pep.

Phylogenomic databases

HOGENOMiHOG000250272.

Enzyme and pathway databases

UniPathwayiUPA00662.

Miscellaneous databases

EvolutionaryTraceiQ9GV41.

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]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGFS_TRYBB
AccessioniPrimary (citable) accession number: Q9GV41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.