ID   P5CR3_BOVIN             Reviewed;         308 AA.
AC   Q58D08;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; BT021789; AAX46636.1; -; mRNA.
DR   EMBL; BC149378; AAI49379.1; -; mRNA.
DR   RefSeq; NP_001014906.1; NM_001014906.1.
DR   AlphaFoldDB; Q58D08; -.
DR   SMR; Q58D08; -.
DR   STRING; 9913.ENSBTAP00000022364; -.
DR   iPTMnet; Q58D08; -.
DR   PaxDb; Q58D08; -.
DR   PeptideAtlas; Q58D08; -.
DR   PRIDE; Q58D08; -.
DR   Ensembl; ENSBTAT00000022364; ENSBTAP00000022364; ENSBTAG00000016810.
DR   GeneID; 512526; -.
DR   KEGG; bta:512526; -.
DR   CTD; 65263; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016810; -.
DR   VGNC; VGNC:33587; PYCR3.
DR   eggNOG; KOG3124; Eukaryota.
DR   GeneTree; ENSGT00950000183044; -.
DR   HOGENOM; CLU_042344_3_0_1; -.
DR   InParanoid; Q58D08; -.
DR   OMA; AKQTCLG; -.
DR   OrthoDB; 952695at2759; -.
DR   Reactome; R-BTA-8964539; Glutamate and glutamine metabolism.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000016810; Expressed in theca cell and 107 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
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.
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..308
FT                   /note="Pyrroline-5-carboxylate reductase 3"
FT                   /id="PRO_0000324560"
SQ   SEQUENCE   308 AA;  32035 MW;  08BD9AD07E567D3D CRC64;
     MAAAAEESGW RRVGFVGAGR MAEAIAQGLI QAGKVEAEHV LASAPSDRNL CRFRAMGCQT
     THSNLEVLHS CSLVFFATKP HILPAVLVEV APAVTAEHIL VSVAAGVSLS TLEKLLPPMA
     RVLRVSPNLP CIVQEGAMVM ARGCCAGSYE AQLLRSLLEA CGQCEEVPEA QVDVHTGLSG
     SGVAFVCAFS EALAEGAIKM GMPSGLAHRI AAQTLLGTAK VLLQKGQHPA QLRTDVCTPG
     GTTIYGLHVL EQGGLRATAM SAVEAATCRA RELSRNPSPV VAQVPSVLQA LQGEGALAHR
     EHSSVARS