P5CR2_BOVIN
ID P5CR2_BOVIN Reviewed; 320 AA.
AC Q17QJ7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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;
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].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118324; AAI18325.1; -; mRNA.
DR RefSeq; NP_001068649.1; NM_001075181.1.
DR AlphaFoldDB; Q17QJ7; -.
DR SMR; Q17QJ7; -.
DR STRING; 9913.ENSBTAP00000000047; -.
DR PaxDb; Q17QJ7; -.
DR PeptideAtlas; Q17QJ7; -.
DR PRIDE; Q17QJ7; -.
DR Ensembl; ENSBTAT00000000047; ENSBTAP00000000047; ENSBTAG00000005835.
DR GeneID; 504987; -.
DR KEGG; bta:504987; -.
DR CTD; 29920; -.
DR VEuPathDB; HostDB:ENSBTAG00000005835; -.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR HOGENOM; CLU_042344_3_0_1; -.
DR InParanoid; Q17QJ7; -.
DR OMA; EQICTPK; -.
DR OrthoDB; 952695at2759; -.
DR Reactome; R-BTA-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000005835; Expressed in retina and 106 other tissues.
DR ExpressionAtlas; Q17QJ7; baseline.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
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_0000270819"
FT REGION 298..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; 33630 MW; 4B43FC3EFC552F91 CRC64;
MSVGFIGAGQ LACALARGFT AAGILSAHKI IASSPEMDLP TVSALRKMGV NLTRSNKETV
RHSDVLFLAV KPHIIPFILD EIGADVQARH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC
MTNTPVLVRE GATVYATGTH ALVEDGQLLE QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY
AFMALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPGQLKDN VCSPGGATIH
ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKISPA ALKKTLLDRV KLESPTVTTL
TPTSSGKLLT RSPVPGGKKD
