ID   P5CR3_RAT               Reviewed;         274 AA.
AC   Q5PQJ6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 3 {ECO:0000312|RGD:1309115};
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:0000312|RGD:1309115}; Synonyms=Pycrl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Enzyme that catalyzes the last step in proline biosynthesis.
CC       Proline is synthesized from either glutamate or ornithine; both are
CC       converted to pyrroline-5-carboxylate (P5C), and then to proline via
CC       pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked
CC       to the conversion of ornithine to proline.
CC       {ECO:0000250|UniProtKB:Q53H96}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC         NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q53H96};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
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; BC087166; AAH87166.1; -; mRNA.
DR   RefSeq; NP_001011993.1; NM_001011993.1.
DR   AlphaFoldDB; Q5PQJ6; -.
DR   SMR; Q5PQJ6; -.
DR   STRING; 10116.ENSRNOP00000053357; -.
DR   jPOST; Q5PQJ6; -.
DR   PaxDb; Q5PQJ6; -.
DR   PRIDE; Q5PQJ6; -.
DR   GeneID; 300035; -.
DR   KEGG; rno:300035; -.
DR   UCSC; RGD:1309115; rat.
DR   CTD; 65263; -.
DR   RGD; 1309115; Pycr3.
DR   VEuPathDB; HostDB:ENSRNOG00000021638; -.
DR   eggNOG; KOG3124; Eukaryota.
DR   HOGENOM; CLU_042344_3_1_1; -.
DR   InParanoid; Q5PQJ6; -.
DR   OMA; AKQTCLG; -.
DR   OrthoDB; 952695at2759; -.
DR   PhylomeDB; Q5PQJ6; -.
DR   Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR   SABIO-RK; Q5PQJ6; -.
DR   UniPathway; UPA00098; UER00361.
DR   PRO; PR:Q5PQJ6; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000054724; Expressed in duodenum and 19 other tissues.
DR   Genevisible; Q5PQJ6; RN.
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   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; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645; PTHR11645; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H96"
FT   CHAIN           2..274
FT                   /note="Pyrroline-5-carboxylate reductase 3"
FT                   /id="PRO_0000324564"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H96"
SQ   SEQUENCE   274 AA;  28878 MW;  0DE4B1076C12B7AE CRC64;
     MADEMSEPRR VGFVGAGRMA EAIAQGLIRA GKVEAKQVLA SAPTDKNLCH FRALGCQTTH
     SNHEVLQNCP LVIFATKPQV LPAVLAEVAP VVTTEHIIVS VAAGISLSSM EELLPPKTRV
     LRVSPNLPCV VQEGAMVMTR GHHAGNEDAK LLQNLLEACG QCIEVPESYV DIHTGLSGSG
     VAFVCTFSEA LAEGAIKMGM PSDLAHRIAA QTLLGTAKML QQEGKHPAQL RTDVLTPAGT
     TIHGLHALEQ GGFRAAAMSA VEAATCRAKE LSKK