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Database: UniProt
Entry: A0A0D2ETV7_9EURO
LinkDB: A0A0D2ETV7_9EURO
Original site: A0A0D2ETV7_9EURO 
ID   A0A0D2ETV7_9EURO        Unreviewed;       290 AA.
AC   A0A0D2ETV7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Pyrroline-5-carboxylate reductase {ECO:0000313|EMBL:KIW77667.1};
GN   ORFNames=Z517_07499 {ECO:0000313|EMBL:KIW77667.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW77667.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW77667.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW77667.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525}.
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DR   EMBL; KN846973; KIW77667.1; -; Genomic_DNA.
DR   RefSeq; XP_013281475.1; XM_013426021.1.
DR   AlphaFoldDB; A0A0D2ETV7; -.
DR   STRING; 1442368.A0A0D2ETV7; -.
DR   GeneID; 25306989; -.
DR   VEuPathDB; FungiDB:Z517_07499; -.
DR   HOGENOM; CLU_042344_1_0_1; -.
DR   OrthoDB; 2104246at2759; -.
DR   Proteomes; UP000053029; Unassembled WGS sequence.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
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   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   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.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT   DOMAIN          11..117
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          183..285
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         15..20
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         73
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         86..89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   290 AA;  31036 MW;  896B29E97408D4F2 CRC64;
     MAIQSTPKPL RVAILGCGFM GTALVQGIID RLDDTCQYDL KFSVSARSSD SIDRLQRKFE
     SHKDRVDIIT SDNTYAARNA EVVFLAFQPQ QLAAIMDSDG PLVQALEGKL LVSILAGVSS
     SQVAQAVIIS PTTQRRVSRA IPSIGAQISE SMTLIADTPL SGPDRDLVSW LFRRVGPIQM
     VPEDLINTAT AVSAACHALT VVAVDAIVDG SVAEGIARPV AHNIAAQCLR SASTLLRDQM
     TIESLKESMS IARGITINAL LQLDRGQVRA GISDAVRFAA QYSKGMSEEK
//
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