ID A0A2Y9LR62_DELLE Unreviewed; 277 AA.
AC A0A2Y9LR62;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN Name=PYCR3 {ECO:0000313|RefSeq:XP_022411181.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022411181.1};
RN [1] {ECO:0000313|RefSeq:XP_022411181.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022411181.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037662}.
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:0000256|ARBA:ARBA00000593};
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:0000256|ARBA:ARBA00000723,
CC ECO:0000256|RuleBase:RU003903};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005205, ECO:0000256|RuleBase:RU003903}.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers.
CC {ECO:0000256|ARBA:ARBA00038523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
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DR RefSeq; XP_022411181.1; XM_022555473.2.
DR AlphaFoldDB; A0A2Y9LR62; -.
DR STRING; 9749.A0A2Y9LR62; -.
DR Ensembl; ENSDLET00000025508; ENSDLEP00000023174; ENSDLEG00000016779.
DR KEGG; dle:111165128; -.
DR InParanoid; A0A2Y9LR62; -.
DR OrthoDB; 196930at2759; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:UniProtKB-EC.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003903}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NADP {ECO:0000256|PIRSR:PIRSR000193-1, ECO:0000256|RuleBase:RU003903};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650,
KW ECO:0000256|RuleBase:RU003903};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 13..107
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 170..274
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 78..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 277 AA; 28810 MW; D67421F899E2B115 CRC64;
MAAVVVAEPG PRRVGFVGAG RMAEAIAQGL IQAGKVEAQH VLASAPTDRN LCRFRALGCQ
TTHSNREVLQ SCSLVFFATK PHILPTVLAE VARVVTAEHI LVSVAAGVSL STLEELLPPM
ARVLRVSPNL PCVVQEGAMV MARGRHAGSG EARLLGTLLE ACGQCEEVPE AQVDVHTGLS
GSGVAFVCAF SEALAEGAIK MGMPSGLAHR IAAQTLLGTA KMLLQKGQHP AQLRTDVCTP
GGTTIYGLHA LEQGGLRAAA MSAVEAATCR ARELSRK
//
