ID   PXL2B_XENLA             Reviewed;         201 AA.
AC   Q6AZG8;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Prostamide/prostaglandin F synthase;
DE            Short=Prostamide/PG F synthase;
DE            Short=Prostamide/PGF synthase;
DE            EC=1.11.1.20 {ECO:0000250|UniProtKB:Q9DB60};
DE   AltName: Full=Peroxiredoxin-like 2B;
GN   Name=prxl2b; Synonyms=fam213b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide H(2)
CC       (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor.
CC       Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha) (By
CC       similarity). {ECO:0000250|UniProtKB:Q9DB60}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + prostaglandin H2 = [thioredoxin]-
CC         disulfide + prostaglandin F2alpha; Xref=Rhea:RHEA:28214, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57404, ChEBI:CHEBI:57405;
CC         EC=1.11.1.20; Evidence={ECO:0000250|UniProtKB:Q9DB60};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + prostamide F2alpha = [thioredoxin]-
CC         dithiol + prostamide H2; Xref=Rhea:RHEA:26373, Rhea:RHEA-COMP:10698,
CC         Rhea:RHEA-COMP:10700, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:53081, ChEBI:CHEBI:53082; EC=1.11.1.20;
CC         Evidence={ECO:0000250|UniProtKB:Q9DB60};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9DB60}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family.
CC       Prostamide/prostaglandin F synthase subfamily. {ECO:0000305}.
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DR   EMBL; BC078028; AAH78028.1; -; mRNA.
DR   RefSeq; NP_001087128.1; NM_001093659.1.
DR   AlphaFoldDB; Q6AZG8; -.
DR   BioGRID; 103877; 1.
DR   MaxQB; Q6AZG8; -.
DR   DNASU; 447017; -.
DR   GeneID; 447017; -.
DR   KEGG; xla:447017; -.
DR   CTD; 447017; -.
DR   Xenbase; XB-GENE-6254580; prxl2b.L.
DR   OMA; QRPVCND; -.
DR   OrthoDB; 1255928at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 447017; Expressed in liver and 20 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR032801; PXL2A/B/C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR28630; PTHR28630; 1.
DR   Pfam; PF13911; AhpC-TSA_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome.
FT   CHAIN           1..201
FT                   /note="Prostamide/prostaglandin F synthase"
FT                   /id="PRO_0000284641"
SQ   SEQUENCE   201 AA;  22013 MW;  DE6A02E0CEB5DA47 CRC64;
     MGSLDLAKAG AILVKNALSG EMVELKSLWK EQTTVLLFLR RFGCQICRWI AKDMGKLKES
     CDVHQIRLVG IGPEEVGLKE FLDGNFFNGE LYIDDSKQSY KDLGFKRYSA LSVIPAALGK
     KVRDIVTKAN ADGVQGNFSG DLLQSGGMLI VSKGGEKVLL HFIQDSPGDY VPLETIVQTL
     GITANVTESQ RPQCNDDVCT R