ID A0A2Y9JAT6_ENHLU Unreviewed; 564 AA.
AC A0A2Y9JAT6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN Name=LOC111146747 {ECO:0000313|RefSeq:XP_022358137.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022358137.1};
RN [1] {ECO:0000313|RefSeq:XP_022358137.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022358137.1};
RG RefSeq;
RL Submitted (SEP-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 -!- 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_022358137.1; XM_022502429.1.
DR AlphaFoldDB; A0A2Y9JAT6; -.
DR STRING; 391180.A0A2Y9JAT6; -.
DR KEGG; elk:111146747; -.
DR OrthoDB; 196930at2759; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000248482; Unplaced.
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:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE 3; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 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};
KW NADP {ECO:0000256|ARBA:ARBA00022857, 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:UP000248482}.
FT DOMAIN 143..237
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 300..404
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT REGION 35..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 58749 MW; 95D875664004C012 CRC64;
MSRWWGVGSG VQALPAPAFH QSQGECFLLE AKLPSSPRRS FPASAASSRG TPTRHAPGRR
PPGQRGTPAL SDPSPLNGAS QAVHTTHPDP ATASSGPEQA ARRNGPADRW PIGWAEGVGR
GTVGSGRGNM AAAVAEPGTS PLRVGFVGAG RMAEAIAQGF IRAGKVEARH ILASAPTDRN
LCHFQALGCQ TTHSNREVLQ NCLLVFFATK PHVLPTVLAE VAPVVTSEHI LVSVAAGVSL
STLEELLPPT ARVLRVSPNL PCVVQEGAMV MARGRHAGSS EAKLLQALLE ACGQCEEVPE
AHVDIHTGLS GSGVAYVCAF SEALAEGAIK MGMPGSLAHR IAAQTLLGTA KMLQQNGQHP
AQLRTDVCTP GGTTIYGLHA LERGGLRAAA MSAVEAATCR ARELSGKQGT APGRWQAQLT
LTTDPWVILK GLLAWPLTEG RDSSAYPHME QPAGNARNLG PKPRPWGLWV DGGLPAAVPP
HYPRGSWSSP TPPRPWSAGT ALAPACRPAD ARPPRGGVCS QSVRRVVAGD TLQQCSPAPA
LHPQPGLPRT SPGASAPDRP GRRE
//