P5CR2_MACFA
ID P5CR2_MACFA Reviewed; 320 AA.
AC Q4R6W7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Pyrroline-5-carboxylate reductase 2;
DE Short=P5C reductase 2;
DE Short=P5CR 2;
DE EC=1.5.1.2;
GN Name=PYCR2; ORFNames=QtsA-16987;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in proline
CC biosynthesis. In some cell types, such as erythrocytes, its primary
CC function may be the generation of NADP(+). Can utilize both NAD and
CC NADP. Has higher affinity for NADP, but higher catalytic efficiency
CC with NADH (By similarity). Involved in cellular response to oxidative
CC stress (By similarity). {ECO:0000250|UniProtKB:Q96C36}.
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:Q96C36};
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:Q96C36};
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:Q96C36}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96C36}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q96C36}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; AB169063; BAE01157.1; -; mRNA.
DR RefSeq; XP_005541057.1; XM_005541000.2.
DR AlphaFoldDB; Q4R6W7; -.
DR SMR; Q4R6W7; -.
DR STRING; 9541.XP_005541057.1; -.
DR Ensembl; ENSMFAT00000067823; ENSMFAP00000017282; ENSMFAG00000031760.
DR GeneID; 101864777; -.
DR KEGG; mcf:101864777; -.
DR CTD; 29920; -.
DR VEuPathDB; HostDB:ENSMFAG00000031760; -.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR OMA; EQICTPK; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000031760; Expressed in bone marrow and 13 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
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; Cytoplasm; Mitochondrion; NADP;
KW Oxidoreductase; Phosphoprotein; Proline biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
FT CHAIN 2..320
FT /note="Pyrroline-5-carboxylate reductase 2"
FT /id="PRO_0000270818"
FT REGION 295..320
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:Q96C36"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
SQ SEQUENCE 320 AA; 33661 MW; 0CD7B0C628866BD7 CRC64;
MSVGIIGAGQ LAYALARGFT AAGIVSAHKI IASSPEMNLP TVSALRKMGV NLTRSNKETV
KHSDVLFLAV KPHIIPFILD EIGADVQARH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC
MTNTPVVVRE GATVYAMGTH ALVEDGQLLE QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY
AFMALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPCQLKDN VCSPGGATIH
ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKISPA ALKKTLLDRV KLESPTVSTL
TPSSPGKLLT RSLALGGKKD
