ID P5CR3_XENLA Reviewed; 274 AA.
AC A1L2Q8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 27-MAR-2024, entry version 71.
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 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] OF 2-274.
RC TISSUE=Olfactory bulb;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) 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; BC129663; AAI29664.1; -; mRNA.
DR AlphaFoldDB; A1L2Q8; -.
DR SMR; A1L2Q8; -.
DR AGR; Xenbase:XB-GENE-6255865; -.
DR Xenbase; XB-GENE-6255865; pycr3.L.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000186698; Genome assembly.
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 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; 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:SF71; 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..274
FT /note="Pyrroline-5-carboxylate reductase 3"
FT /id="PRO_0000324566"
SQ SEQUENCE 274 AA; 28875 MW; 9BE2A785FE78184F CRC64;
MAASPRVSLP VGCIGAGRMA QGILEGILHK GEITPQNVMV SAPTDRNLEK LKARGCCTSH
DNRSVVSNCR VVFLATKPHI IPSVLQEIYP KVTADHLIIS MAAGVTLETL EKNLPPGSKV
IRMMPNLPCV LQEGAIVFSR GRCAGEVEAD VFESLVRTCG LCVEVPQSCI DIHTGVSGSG
VAYVYTFAEA LADGAVKMGM PSALARQIVA QTLLGAGKML LQSEEHPASL RADVCTPGGT
TIFGLHELEK GGLRAAVMNA VEAATTRAMD MGRK
//
