ID Q8I6L9_TRYCR Unreviewed; 379 AA. AC Q8I6L9; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 61. DE SubName: Full=Prostaglandin F2a synthase {ECO:0000313|EMBL:BAC24024.1}; DE SubName: Full=Prostaglandin F2alpha synthase {ECO:0000313|EMBL:KAF5213788.1}; GN Name=TcPGFS {ECO:0000313|EMBL:BAC24024.1}; GN ORFNames=ECC02_012910 {ECO:0000313|EMBL:KAF5214483.1}, ECC02_013670 GN {ECO:0000313|EMBL:KAF5213788.1}; OS Trypanosoma cruzi. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum. OX NCBI_TaxID=5693 {ECO:0000313|EMBL:BAC24024.1}; RN [1] {ECO:0000313|EMBL:BAC24024.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12417633; DOI=10.1084/jem.20020885; RA Kubata B.K., Kabututu Z., Nozaki T., Munday C.J., Fukuzumi S., Ohkubo K., RA Lazarus M., Maruyama T., Martin S.K., Duszenko M., Urade Y.; RT "A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma RT cruzi."; RL J. Exp. Med. 196:1241-1251(2002). RN [2] {ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FMN. RX PubMed=21840922; DOI=10.1093/jb/mvr096; RA Okamoto N., Yamaguchi K., Mizohata E., Tokuoka K., Uchiyama N., RA Sugiyama S., Matsumura H., Inaka K., Urade Y., Inoue T.; RT "Structural insight into the stereoselective production of PGF2alpha by Old RT Yellow Enzyme from Trypanosoma cruzi."; RL J. Biochem. 150:563-568(2011). RN [3] {ECO:0000313|EMBL:KAF5213788.1, ECO:0000313|Proteomes:UP000583944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berenice {ECO:0000313|EMBL:KAF5213788.1, RC ECO:0000313|Proteomes:UP000583944}; RX PubMed=31218350; RA Diaz-Viraque F., Pita S., Greif G., de Souza R.C.M., Iraola G., Robello C.; RT "Nanopore Sequencing Significantly Improves Genome Assembly of the RT Protozoan Parasite Trypanosoma cruzi."; RL Genome Biol. Evol. 11:1952-1957(2019). RN [4] {ECO:0000313|EMBL:KAF5213788.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berenice {ECO:0000313|EMBL:KAF5213788.1}; RA Diaz Viraque F.; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB075599; BAC24024.1; -; mRNA. DR EMBL; JABDHM010000747; KAF5213788.1; -; Genomic_DNA. DR EMBL; JABDHM010000495; KAF5214483.1; -; Genomic_DNA. DR PDB; 3ATY; X-ray; 1.70 A; A/B=1-379. DR PDB; 3ATZ; X-ray; 2.04 A; A/B/C/D=1-379. DR PDBsum; 3ATY; -. DR PDBsum; 3ATZ; -. DR VEuPathDB; TriTrypDB:C3747_204g20; -. DR VEuPathDB; TriTrypDB:C4B63_280g10; -. DR VEuPathDB; TriTrypDB:ECC02_012910; -. DR VEuPathDB; TriTrypDB:ECC02_013670; -. DR VEuPathDB; TriTrypDB:Tc_MARK_5765; -. DR VEuPathDB; TriTrypDB:TcBrA4_0060960; -. DR VEuPathDB; TriTrypDB:TcBrA4_0061040; -. DR VEuPathDB; TriTrypDB:TcCL_ESM09001; -. DR VEuPathDB; TriTrypDB:TcCLB.507617.9; -. DR VEuPathDB; TriTrypDB:TcCLB.508461.80; -. DR VEuPathDB; TriTrypDB:TCDM_09004; -. DR VEuPathDB; TriTrypDB:TcG_08968; -. DR VEuPathDB; TriTrypDB:TCSYLVIO_007017; -. DR VEuPathDB; TriTrypDB:TcYC6_0070580; -. DR Proteomes; UP000583944; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR CDD; cd02933; OYE_like_FMN; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001155; OxRdtase_FMN_N. DR InterPro; IPR045247; Oye-like. DR PANTHER; PTHR22893; NADH OXIDOREDUCTASE-RELATED; 1. DR PANTHER; PTHR22893:SF110; NADPH DEHYDROGENASE 2-RELATED; 1. DR Pfam; PF00724; Oxidored_FMN; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ}; KW Flavoprotein {ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ}; KW FMN {ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ}; KW Nucleotide-binding {ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ}. FT DOMAIN 7..356 FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00724" FT BINDING 26 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 28 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 61 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 103 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 249 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 313 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 315 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 336 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" FT BINDING 337 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:3ATY, ECO:0007829|PDB:3ATZ" SQ SEQUENCE 379 AA; 42261 MW; 4EEC57419ACAF8CE CRC64; MATFPELLRP LKLGRYTLRN RIIMAPLTRC QATEDDHVPR TESMLKYYED RASAGLIIAE ATMVQPNYTG FLTEPGIYSD AQIEEWRKIV DAVHKKGGLI FLQLIHAGRA GIPEKILQQS KSDQDPLAGR LLAASAIPIK DHRIPAYFAA SGEKETYGVP EELTDDEVRD GIIPLFVEGA KNAIFKAGFD GVEIHGANGY LLDAFFRESS NKRQSGPYAG TTIDTRCQLI YDVTKSVCDA VGSDRVGLRI SPLNGVHGMI DSNPEALTKH LCKKIEPLSL AYLHYLRGDM VNQQIGDVVA WVRGSYSGVK ISNLRYDFEE ADQQIREGKV DAVAFGAKFI ANPDLVERAQ QNWPLNEPRP ETYYTRTAVG YNDYPTYNK //