ID   PXL2B_XENTR             Reviewed;         201 AA.
AC   Q28IJ3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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; ORFNames=TNeu028h04.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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; CR760360; CAJ83264.1; -; mRNA.
DR   RefSeq; NP_001017220.1; NM_001017220.2.
DR   AlphaFoldDB; Q28IJ3; -.
DR   STRING; 8364.ENSXETP00000045936; -.
DR   PaxDb; Q28IJ3; -.
DR   Ensembl; ENSXETT00000045936; ENSXETP00000045936; ENSXETG00000021242.
DR   GeneID; 549974; -.
DR   KEGG; xtr:549974; -.
DR   CTD; 127281; -.
DR   Xenbase; XB-GENE-968463; prxl2b.
DR   eggNOG; KOG4498; Eukaryota.
DR   HOGENOM; CLU_094994_0_0_1; -.
DR   InParanoid; Q28IJ3; -.
DR   OMA; CGGLCQQ; -.
DR   OrthoDB; 1255928at2759; -.
DR   PhylomeDB; Q28IJ3; -.
DR   TreeFam; TF313804; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000021242; Expressed in neurula embryo and 12 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IBA:GO_Central.
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_0000284642"
SQ   SEQUENCE   201 AA;  21982 MW;  11843C3F60243E88 CRC64;
     MASVDLAKVG TILVKNALSG EMVELKSLWK EKTTVLLFLR RFGCQICRWI AKDIGKLKAS
     CDAHQIRLVG IGPEEVGLKE FLEGNFFNGE LYIDESKESY KTLGFKRYSA LSVIPAALGK
     KVRDIVTKAN ADGVQGNFSG DLLQSGGMLI VSKGGEKVLL HFIQDSPGDY VPLESIVQTL
     GITANVTESQ RPQCNDEVCT R