ID   P5CR3_DANRE             Reviewed;         288 AA.
AC   Q5SPD7; Q05AI4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 3 {ECO:0000250|UniProtKB:Q53H96};
DE            Short=P5C reductase 3;
DE            Short=P5CR 3;
DE            EC=1.5.1.2 {ECO:0000250|UniProtKB:Q53H96};
DE   AltName: Full=Pyrroline-5-carboxylate reductase-like protein;
GN   Name=pycr3 {ECO:0000250|UniProtKB:Q53H96}; Synonyms=pycrl;
GN   ORFNames=si:dkey-235d18.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-288.
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Oxidoreductase that catalyzes the last step in proline
CC       biosynthesis, which corresponds to the reduction of pyrroline-5-
CC       carboxylate (P5C) to L-proline using NAD(P)H. Proline is synthesized
CC       from either glutamate or ornithine; both are converted to P5C, and then
CC       to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCR3 is
CC       exclusively linked to the biosynthesis of proline from ornithine.
CC       {ECO:0000250|UniProtKB:Q53H96}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NADP(+) = (S)-1-pyrroline-5-carboxylate + NADPH +
CC         2 H(+); Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q53H96};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14111;
CC         Evidence={ECO:0000250|UniProtKB:Q53H96};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NAD(+) = (S)-1-pyrroline-5-carboxylate + NADH + 2
CC         H(+); Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q53H96};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14107;
CC         Evidence={ECO:0000250|UniProtKB:Q53H96};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000250|UniProtKB:Q53H96}.
CC   -!- SUBUNIT: Homodecamer; composed of 5 homodimers.
CC       {ECO:0000250|UniProtKB:P32322}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q53H96}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AL929003; CAI21008.1; -; Genomic_DNA.
DR   EMBL; BC124544; AAI24545.1; -; mRNA.
DR   RefSeq; NP_001038403.1; NM_001044938.1.
DR   AlphaFoldDB; Q5SPD7; -.
DR   SMR; Q5SPD7; -.
DR   FunCoup; Q5SPD7; 242.
DR   STRING; 7955.ENSDARP00000011713; -.
DR   GlyGen; Q5SPD7; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7955-ENSDARP00000011713; -.
DR   PeptideAtlas; Q5SPD7; -.
DR   Ensembl; ENSDART00000002787; ENSDARP00000011713; ENSDARG00000015236.
DR   GeneID; 560682; -.
DR   KEGG; dre:560682; -.
DR   AGR; ZFIN:ZDB-GENE-041014-244; -.
DR   CTD; 65263; -.
DR   ZFIN; ZDB-GENE-041014-244; pycr3.
DR   eggNOG; KOG3124; Eukaryota.
DR   GeneTree; ENSGT00950000183044; -.
DR   HOGENOM; CLU_042344_3_0_1; -.
DR   InParanoid; Q5SPD7; -.
DR   OMA; AKQTCLG; -.
DR   OrthoDB; 10263291at2759; -.
DR   PhylomeDB; Q5SPD7; -.
DR   Reactome; R-DRE-8964539; Glutamate and glutamine metabolism.
DR   UniPathway; UPA00098; UER00361.
DR   PRO; PR:Q5SPD7; -.
DR   Proteomes; UP000000437; Chromosome 20.
DR   Bgee; ENSDARG00000015236; Expressed in mature ovarian follicle and 23 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:UniProtKB.
DR   GO; GO:0055129; P:L-proline biosynthetic process; ISS:UniProtKB.
DR   FunFam; 3.40.50.720:FF:000367; Pyrroline-5-carboxylate reductase; 1.
DR   FunFam; 1.10.3730.10:FF:000003; Pyrroline-5-carboxylate reductase 1, mitochondrial; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR   HAMAP; MF_01925; P5C_reductase; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR053790; P5CR-like_CS.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   NCBIfam; TIGR00112; proC; 1.
DR   PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE 3; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..288
FT                   /note="Pyrroline-5-carboxylate reductase 3"
FT                   /id="PRO_0000324565"
SQ   SEQUENCE   288 AA;  29922 MW;  31A523F549C35D60 CRC64;
     MSLSGASDKT SDSPDVFQIK IGFIGAGNMA FGVAQGIIAS GKVPPSNIII SAPSMNNLPR
     FKEKGVSVTH SNHEVVGGSR LIFLAVKPHI IPQVLKEISQ EVTKEHIIVS MAAGITIATL
     EELLPAGTHV IRIMPNLPCM LLEGALLLSC GSHAGEQEET LLKTLLGPCG LVEFGPESWI
     DAHVGLSGSG VAFVYVFAEA LADGAVKMGM PSTLARRIAA QTILGAGVLL RDSGKLPAEL
     KAEVCTPGGT TIHGIHALEK GGFRAAAIGA VEAASERARE LGNKQKKN
//