PGFS_TRYBB
ID PGFS_TRYBB Reviewed; 276 AA.
AC Q9GV41;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=9,11-endoperoxide prostaglandin H2 reductase {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:11067881};
DE AltName: Full=Prostaglandin F2-alpha synthase;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=MITat 1.4;
RX PubMed=11067881; DOI=10.1084/jem.192.9.1327;
RA Kubata B.K., Duszenko M., Kabututu Z., Rawer M., Szallies A., Fujimori K.,
RA Inui T., Nozaki T., Yamashita K., Horii T., Urade Y., Hayaishi O.;
RT "Identification of a novel prostaglandin f(2alpha) synthase in Trypanosoma
RT brucei.";
RL J. Exp. Med. 192:1327-1338(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP.
RA Inoue T.;
RT "The crystal structure of prostaglandin F synthase from Trypanosoma
RT brucei.";
RL Submitted (FEB-2004) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NADP-dependent formation of prostaglandin F2-
CC alpha from prostaglandin H2. Has also aldo/ketoreductase activity
CC towards the synthetic substrates 9,10-phenanthrenequinone and p-
CC nitrobenzaldehyde. {ECO:0000269|PubMed:11067881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:11067881};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for prostaglandin H2 {ECO:0000269|PubMed:11067881};
CC KM=0.42 uM for 9,10-phenanthrenequinone
CC {ECO:0000269|PubMed:11067881};
CC KM=0.8 uM for p-nitrobenzaldehyde {ECO:0000269|PubMed:11067881};
CC KM=5.7 uM for NADPH {ECO:0000269|PubMed:11067881};
CC Vmax=2 umol/min/mg enzyme toward prostaglandin H2
CC {ECO:0000269|PubMed:11067881};
CC Vmax=22 umol/min/mg enzyme toward p-nitrobenzaldehyde
CC {ECO:0000269|PubMed:11067881};
CC Vmax=48 umol/min/mg enzyme toward 9,10-phenanthrenequinone
CC {ECO:0000269|PubMed:11067881};
CC pH dependence:
CC Optimum pH is 6-9. {ECO:0000269|PubMed:11067881};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11067881, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11067881}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB034727; BAB17681.1; -; mRNA.
DR PDB; 1VBJ; X-ray; 2.10 A; A/B=1-276.
DR PDBsum; 1VBJ; -.
DR AlphaFoldDB; Q9GV41; -.
DR SMR; Q9GV41; -.
DR DrugBank; DB04272; Citric acid.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR SABIO-RK; Q9GV41; -.
DR UniPathway; UPA00662; -.
DR EvolutionaryTrace; Q9GV41; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISM:GeneDB.
DR GO; GO:0045290; F:D-arabinose 1-dehydrogenase [NAD(P)+] activity; TAS:GeneDB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; IEA:RHEA.
DR GO; GO:0019571; P:D-arabinose catabolic process; TAS:GeneDB.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd19156; AKR_AKR5A1_2; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044499; AKR5A.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; PTHR43827; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NADP; Nucleotide-binding; Oxidoreductase;
KW Prostaglandin biosynthesis; Prostaglandin metabolism.
FT CHAIN 1..276
FT /note="9,11-endoperoxide prostaglandin H2 reductase"
FT /id="PRO_0000419493"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 22..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139..140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 187..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 230..232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 236..240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT SITE 77
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:1VBJ"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1VBJ"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:1VBJ"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:1VBJ"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:1VBJ"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1VBJ"
SQ SEQUENCE 276 AA; 30993 MW; D57ECDCCEE8B6971 CRC64;
MALTQSLKLS NGVMMPVLGF GMWKLQDGNE AETATMWAIK SGYRHIDTAA IYKNEESAGR
AIASCGVPRE ELFVTTKLWN SDQGYESTLS AFEKSIKKLG LEYVDLYLIH WPGKDKFIDT
WKAFEKLYAD KKVRAIGVSN FHEHHIEELL KHCKVAPMVN QIELHPLLNQ KALCEYCKSK
NIAVTAWSPL GQGHLVEDAR LKAIGGKYGK TAAQVMLRWE IQAGVITIPK SGNEARIKEN
GNIFDFELTA EDIQVIDGMN AGHRYGPDPE VFMNDF
