ID   P5CR1_PONAB             Reviewed;         319 AA.
AC   Q5R9X6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 1, mitochondrial;
DE            Short=P5C reductase 1;
DE            Short=P5CR 1;
DE            EC=1.5.1.2;
GN   Name=PYCR1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in proline
CC       biosynthesis. Can utilize both NAD and NADP, but has higher affinity
CC       for NAD. Involved in the cellular response to oxidative stress.
CC       {ECO:0000250|UniProtKB:P32322}.
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:P32322};
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:P32322};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC   -!- SUBUNIT: Homodecamer; composed of 5 homodimers. Interacts with LTO1.
CC       {ECO:0000250|UniProtKB:P32322}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P32322}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; CR859254; CAH91434.1; -; mRNA.
DR   RefSeq; NP_001125842.1; NM_001132370.1.
DR   AlphaFoldDB; Q5R9X6; -.
DR   SMR; Q5R9X6; -.
DR   STRING; 9601.ENSPPYP00000009827; -.
DR   GeneID; 100172771; -.
DR   CTD; 5831; -.
DR   eggNOG; KOG3124; Eukaryota.
DR   InParanoid; Q5R9X6; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006561; P: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   Acetylation; Amino-acid biosynthesis; Mitochondrion; NADP; Oxidoreductase;
KW   Phosphoprotein; Proline biosynthesis; Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P32322"
FT   CHAIN           2..319
FT                   /note="Pyrroline-5-carboxylate reductase 1, mitochondrial"
FT                   /id="PRO_0000187316"
FT   REGION          294..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         95..97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32322"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32322"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32322"
SQ   SEQUENCE   319 AA;  33361 MW;  9E8C4DED0638EFC5 CRC64;
     MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV
     QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC
     MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY
     AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH
     ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL
     SPSGHTKLLP RSLAPAGKD