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Database: UniProt
Entry: A0A183AYW7_9TREM
LinkDB: A0A183AYW7_9TREM
Original site: A0A183AYW7_9TREM 
ID   A0A183AYW7_9TREM        Unreviewed;       209 AA.
AC   A0A183AYW7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|ARBA:ARBA00012855, ECO:0000256|RuleBase:RU003903};
DE            EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855, ECO:0000256|RuleBase:RU003903};
GN   ORFNames=ECPE_LOCUS12152 {ECO:0000313|EMBL:VDP89397.1};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0001218801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0001218801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP89397.1, ECO:0000313|Proteomes:UP000272942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Egypt {ECO:0000313|EMBL:VDP89397.1,
RC   ECO:0000313|Proteomes:UP000272942};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; UZAN01052249; VDP89397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183AYW7; -.
DR   WBParaSite; ECPE_0001218801-mRNA-1; ECPE_0001218801-mRNA-1; ECPE_0001218801.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000050740; Unplaced.
DR   Proteomes; UP000272942; Unassembled WGS sequence.
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; 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|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:UP000272942}.
FT   DOMAIN          1..39
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          103..206
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
SQ   SEQUENCE   209 AA;  21673 MW;  33146885FCA855D9 CRC64;
     MAKKSDVILA CVKPNVILSA LSEIAKELDS KLVVSVAAGI TLEQMKQVVP KTTRLVRIMP
     NTPCLVQAGT AIFSRGATVT NEDIAMTTSL CSSIFNVFEE IPESLINAAS GISGCGPAYM
     FLIAEALADG GVRMGVPRPL AHKLAVSTMF GAAAMMEKTG ENPSKLKNDV CSPGGATIAA
     VHALEEGGVR AAIMNAVQAA AVRSEEISK
//
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